(data stored in ACNUC7421 zone)

SWISSPROT: GLMU_BACSU

ID   GLMU_BACSU              Reviewed;         456 AA.
AC   P14192; Q45684;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   11-DEC-2019, entry version 142.
DE   RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631};
DE   Includes:
DE     RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631};
DE              EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631};
DE     AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE   Includes:
DE     RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE              EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631};
GN   Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; Synonyms=gcaD, tms, tms-26;
GN   OrderedLocusNames=BSU00500;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2555671; DOI=10.1007/bf00332425;
RA   Nilsson D., Hove-Jensen B., Arnvig K.;
RT   "Primary structure of the tms and prs genes of Bacillus subtilis.";
RL   Mol. Gen. Genet. 218:565-571(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC   STRAIN=168;
RX   PubMed=6181373; DOI=10.1007/bf00729452;
RA   Moran C.P. Jr., Lang N., LeGrice S.F.J., Lee G., Stephens M.,
RA   Sonenshein A.L., Pero J., Losick R.;
RT   "Nucleotide sequences that signal the initiation of transcription and
RT   translation in Bacillus subtilis.";
RL   Mol. Gen. Genet. 186:339-346(1982).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC   STRAIN=168;
RX   PubMed=1373326; DOI=10.1016/0167-4781(92)90536-9;
RA   Hudspeth D.S.S., Vary P.S.;
RT   "spoVG sequence of Bacillus megaterium and Bacillus subtilis.";
RL   Biochim. Biophys. Acta 1130:229-231(1992).
CC   -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo
CC       biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-
CC       terminal domain catalyzes the transfer of acetyl group from acetyl
CC       coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-
CC       acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into
CC       UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-
CC       triphosphate), a reaction catalyzed by the N-terminal domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01631}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-
CC         acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC         diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01631};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC       alpha-D-glucosamine 6-phosphate (route II): step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01631}.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC       acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01631}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01631}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01631}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}.
DR   EMBL; X16518; CAA34522.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05285.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11826.1; -; Genomic_DNA.
DR   EMBL; J01550; AAA22854.1; -; Genomic_DNA.
DR   EMBL; X62378; CAA44243.1; -; Genomic_DNA.
DR   PIR; S66080; S66080.
DR   RefSeq; NP_387931.1; NC_000964.3.
DR   SMR; P14192; -.
DR   STRING; 224308.BSU00500; -.
DR   jPOST; P14192; -.
DR   PaxDb; P14192; -.
DR   PRIDE; P14192; -.
DR   EnsemblBacteria; CAB11826; CAB11826; BSU00500.
DR   GeneID; 936139; -.
DR   KEGG; bsu:BSU00500; -.
DR   PATRIC; fig|224308.43.peg.51; -.
DR   eggNOG; ENOG4105CAJ; Bacteria.
DR   eggNOG; COG1207; LUCA.
DR   HOGENOM; HOG000283476; -.
DR   InParanoid; P14192; -.
DR   KO; K04042; -.
DR   BioCyc; BSUB:BSU00500-MONOMER; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00113; UER00533.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03353; LbH_GlmU_C; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_01631; GlmU; 1.
DR   InterPro; IPR005882; Bifunctional_GlmU.
DR   InterPro; IPR038009; GlmU_C_LbH.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 3.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01173; glmU; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; P14192.
DR   SWISS-2DPAGE; P14192.
KW   Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW   Peptidoglycan synthesis; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..456
FT                   /note="Bifunctional protein GlmU"
FT                   /id="PRO_0000068706"
FT   REGION          1..230
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          9..12
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          78..79
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          231..251
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          252..456
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          386..387
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   ACT_SITE        363
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   METAL           103
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   METAL           228
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         23
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         73
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         140
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         155
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         170
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         228
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         333
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         351
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         366
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         377
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         423
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         440
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   CONFLICT        19
FT                   /note="S -> L (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71..72
FT                   /note="RV -> AL (in Ref. 2; BAA05285/CAB11826)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="R -> A (in Ref. 2; BAA05285/CAB11826)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   456 AA;  49610 MW;  6D65E0A05D5E9261 CRC64;
     MDKRFAVVLA AGQGTRMKSK LYKVLHPVCG KPMVEHVVDE ALKLSLSKLV TIVGHGAEEV
     KKQLGDKSEY RVQAKQLGTA HAVKQAQPFL ADEKGVTIVI CGDTPLLTAE TMEQMLKEHT
     QREAKRTILT AVAEDPTGYG RIIRSENGAV QKIVEHKDAS EEERLVTEIN TGTYCFDNEA
     LFRAIDQVSN DNAQGEYYLP DVIEILKNEG ETVAAYQTGN FQETLGVNDR VALSQAEQFM
     KERINKRHMQ NGVTLIDPMN TYISPDAVIG SDTVIYPGTV IKGEVQIGED TIIGPHTEIM
     NSAIGSRTVI KQSVVNHSKV GNDVNIGPFA HIRPDSVIGN EVKIGNFVEI KKTQFGDRSK
     ASHLSYVGDA EVGTDVNLGC GSITVNYDGK NKYLTKIEDG AFIGCNSNLV APVTVGEGAY
     VAAGSTVTED VPGKALAIAR ARQVNKDDYV KNIHKK
//

If you have problems or comments...

PBIL Back to PBIL home page