(data stored in ACNUC7421 zone)

SWISSPROT: GLMU_RHILO

ID   GLMU_RHILO              Reviewed;         458 AA.
AC   Q98LX2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 105.
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}; OrderedLocusNames=mll0836;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB48341.1; -; Genomic_DNA.
DR   RefSeq; WP_010909696.1; NC_002678.2.
DR   SMR; Q98LX2; -.
DR   STRING; 266835.14021729; -.
DR   EnsemblBacteria; BAB48341; BAB48341; BAB48341.
DR   KEGG; mlo:mll0836; -.
DR   PATRIC; fig|266835.9.peg.666; -.
DR   eggNOG; ENOG4105CAJ; Bacteria.
DR   eggNOG; COG1207; LUCA.
DR   HOGENOM; HOG000283476; -.
DR   KO; K04042; -.
DR   OMA; QNAQKEY; -.
DR   OrthoDB; 1381953at2; -.
DR   BioCyc; MLOT266835:G1G20-679-MONOMER; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00113; UER00533.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000552; 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; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01173; glmU; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q98LX2.
DR   SWISS-2DPAGE; Q98LX2.
KW   Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW   Peptidoglycan synthesis; Repeat; Transferase.
FT   CHAIN           1..458
FT                   /note="Bifunctional protein GlmU"
FT                   /id="PRO_0000233831"
FT   REGION          1..232
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          11..14
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          83..84
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          233..253
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          254..458
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          372..373
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   METAL           108
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   METAL           230
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         25
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         78
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         144
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         158
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         173
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         230
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         319
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         337
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         352
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         363
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         366
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         391
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         409
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         426
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
SQ   SEQUENCE   458 AA;  47737 MW;  523AA4C5D4E9D1DE CRC64;
     MSQRSCLSVI LAAGEGTRMK SALPKVLHQI AGLPMVAHVV KAADAAGASS DAIVIGHGAE
     EMRKAVTKFS PKAETFVQEE RLGTAHAVLA AREAISRGYD DILVMFGDTP LIDAEALNLA
     RLKLAEGAAV AVIGFRPPLP NGYGRLVEKG GKLIAIREEK DCSEAEKKIG FCNAGMMAVA
     GAHALKLLDA VGNKNAKGEY YLTDIVEIAG AQGLDVVATE ASFENALGIN NRAELAQAEG
     IWQARRRQEA MLSGVTLIAP ETVYFSHDTE IGADTVVEPN VWFGPGVKIA GGAKIHAFSH
     IEGATIAANC DVGPFARLRP GADLRNKAKV GNFCEVKQAV IEEGAKVNHL TYIGDARVGA
     GANIGAGTIT CNYDGFSKFF TDIGEGAFVG SNSSLVAPVS IGKGGYIASG SVITESVPDD
     ALAFGRARQK TIPGKGKELR ERFASAAAAK KKAAGADH
//

If you have problems or comments...

PBIL Back to PBIL home page