(data stored in ACNUC7421 zone)

SWISSPROT: GLMU_THEFY

ID   GLMU_THEFY              Reviewed;         484 AA.
AC   Q47SW5;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 96.
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};
GN   OrderedLocusNames=Tfu_0414;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes the last two sequential reactions in the de
CC       novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-
CC       GlcNAc). The C-terminal domain catalyzes the transfer of acetyl
CC       group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P)
CC       to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is
CC       converted into UDP-GlcNAc by the transfer of uridine 5-
CC       monophosphate (from uridine 5-triphosphate), a reaction catalyzed
CC       by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+)
CC         + N-acetyl-alpha-D-glucosamine 1-phosphate;
CC         Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516;
CC         EC=2.3.1.157; 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;
CC         Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776;
CC         EC=2.7.7.23; 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-
CC       Rule:MF_01631};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate
CC       from 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.
CC       {ECO:0000255|HAMAP-Rule:MF_01631}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
CC       biosynthesis. {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; CP000088; AAZ54452.1; -; Genomic_DNA.
DR   RefSeq; WP_011290861.1; NC_007333.1.
DR   SMR; Q47SW5; -.
DR   STRING; 269800.Tfu_0414; -.
DR   EnsemblBacteria; AAZ54452; AAZ54452; Tfu_0414.
DR   KEGG; tfu:Tfu_0414; -.
DR   eggNOG; ENOG4105CAJ; Bacteria.
DR   eggNOG; COG1207; LUCA.
DR   HOGENOM; HOG000283476; -.
DR   KO; K04042; -.
DR   OMA; IEPQTHL; -.
DR   OrthoDB; 1381953at2; -.
DR   BioCyc; TFUS269800:G1G4Q-420-MONOMER; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00113; UER00533.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000434; 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; 2.
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; Q47SW5.
DR   SWISS-2DPAGE; Q47SW5.
KW   Acyltransferase; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nucleotidyltransferase;
KW   Peptidoglycan synthesis; Reference proteome; Repeat; Transferase.
FT   CHAIN         1    484       Bifunctional protein GlmU.
FT                                /FTId=PRO_0000233867.
FT   REGION        1    240       Pyrophosphorylase. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       12     15       UDP-GlcNAc binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       84     85       UDP-GlcNAc binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      241    261       Linker. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      262    484       N-acetyltransferase. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      396    397       Acetyl-CoA binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   ACT_SITE    373    373       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   METAL       113    113       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   METAL       238    238       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING      26     26       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING      79     79       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     150    150       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01631}.
FT   BINDING     165    165       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     180    180       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     238    238       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     343    343       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     361    361       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     376    376       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     387    387       UDP-GlcNAc. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     390    390       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01631}.
FT   BINDING     415    415       Acetyl-CoA. {ECO:0000255|HAMAP-
FT                                Rule:MF_01631}.
FT   BINDING     433    433       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01631}.
SQ   SEQUENCE   484 AA;  51144 MW;  7DC2340EE96F77AC CRC64;
     MSASRPAAVM VLAAGEGTRM KSRRPKVLHE ICGRSLLGHV LAAVAELEPQ RTVVVVGHAR
     EQVTEHLKSI APHAITALQE EQKGTGHAVR MAIEALRAQN VELTGTVVLT CGDTPLLRGA
     TLRDLVAAHE AEGNAVTILS ARVPDPTGYG RIVRDAAGAV TGIVEHADAT EEQRAVDEIN
     SGMYAFDGAL LSQVVHRLSA DNAKGEEYIT DAVALLRGDG HRVGAYIAPD RTEVEGVNDR
     VQLAEARRLL NARLLEQLMR DGVTVVDPAS TWVDVDVRVG RDAVLEPQTQ LQGRTVIGEG
     AQVGPATVLC DTEVGEDAVV SHTVAREAVI GPEATVGPYA YLRPGARLDR GVKIGTFVEV
     KNSTVGEGSK VPHLTYVGDA DIGKGVNIGA SSVFVNYDGV NKHRTVIGDY ARTGSDTMFV
     APVRVGDGAY TGAGTVVRED VPPGALAVSA GPQRTIEGWV ERKRPGTPAA QAAERARARS
     EEDR
//

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