(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHK1_GEOS0

ID   A0A0F6BHK1_GEOS0        Unreviewed;       459 AA.
AC   A0A0F6BHK1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 34.
DE   RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631};
DE   Includes:
DE     RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01631};
DE              EC=2.7.7.23 {ECO:0000256|HAMAP-Rule:MF_01631};
DE     AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
DE   Includes:
DE     RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
DE              EC=2.3.1.157 {ECO:0000256|HAMAP-Rule:MF_01631};
GN   Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631};
GN   OrderedLocusNames=GY4MC1_0046 {ECO:0000313|EMBL:ADP72902.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72902.1};
RN   [1] {ECO:0000313|EMBL:ADP72902.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72902.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00381483}.
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:0000256|HAMAP-Rule:MF_01631,
CC         ECO:0000256|SAAS:SAAS01124206};
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:0000256|HAMAP-Rule:MF_01631,
CC         ECO:0000256|SAAS:SAAS01124218};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01631};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01631};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083707}.
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:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083565}.
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:0000256|HAMAP-
CC       Rule:MF_01631, ECO:0000256|SAAS:SAAS00083673}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00569615}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00083712}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00569628}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00569629}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}.
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DR   EMBL; CP002293; ADP72902.1; -; Genomic_DNA.
DR   RefSeq; WP_003247439.1; NC_014650.1.
DR   EnsemblBacteria; ADP72902; ADP72902; GY4MC1_0046.
DR   GeneID; 29237333; -.
DR   KEGG; gmc:GY4MC1_0046; -.
DR   KO; K04042; -.
DR   OMA; QNAQKEY; -.
DR   OrthoDB; 1381953at2; -.
DR   BioCyc; GSP581103:G1GOQ-57-MONOMER; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
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; A0A0F6BHK1.
DR   SWISS-2DPAGE; A0A0F6BHK1.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458646};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00083584};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458644};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00458650};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00458735};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458606};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00083642};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458661};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458685};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00458660};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458747}.
FT   DOMAIN          6..206
FT                   /note="NTP_transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   REGION          1..230
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          9..12
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          78..79
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          231..251
FT                   /note="Linker"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          252..459
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          386..387
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   ACT_SITE        363
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   METAL           103
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   METAL           228
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         23
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         73
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         140
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         155
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         170
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         228
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         333
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         351
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         366
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         377
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         423
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         440
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
SQ   SEQUENCE   459 AA;  49326 MW;  1D0C59DCD815BD5A CRC64;
     MVKRYAVILA AGQGTRMKSK QYKVLHPVCG KPMVQHVVDQ VLQLGIEKLI TVVGFGAEQV
     KMQLGDQSEY AFQQEQLGTA HAVMQAASHL HGKDGVTLVV CGDTPLITAE TMQALLDHHL
     ATKAKATVLT AIADNPAGYG RIVRDSHGNV AKIVEHKDAS EQERAIKEIN TGTYCFDNKS
     LFEALTHVSN NNVQGEYYLT DVIEILKSNG GIISAYEAPS FEETIGVNDR AALAEAEKIM
     RARICRKHML NGVTIIDPAH TYISAEAQIG RDTVIYPGTV IEGKTVIGED CIIGPNSEIK
     DCLIGNGTTI RHSVAHDSEI GNDVTIGPFA HIRPLSKIAD EVRIGNFVEV KKSVFGKGSK
     ASHLSYIGDA EIGADVNLGC GSITVNYDGK NKHMTKIEDG AFIGCNVNLI APVTVGKGAY
     VAAGSTITDD VPANALSIAR ARQVNKENYV DRLSIKKNS
//

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