(data stored in SCRATCH zone)

SWISSPROT: C8W302_DESAS

ID   C8W302_DESAS            Unreviewed;       458 AA.
AC   C8W302;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Bifunctional protein GlmU {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};
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};
GN   Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631};
GN   OrderedLocusNames=Dtox_0205 {ECO:0000313|EMBL:ACV61158.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61158.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61158.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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:0000256|HAMAP-Rule:MF_01631,
CC       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;
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:0000256|HAMAP-Rule:MF_01631,
CC         ECO:0000256|SAAS:SAAS01124206};
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:0000256|HAMAP-Rule:MF_01631,
CC         ECO:0000256|SAAS:SAAS01124218};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01631};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01631};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00083707}.
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: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.
CC       {ECO:0000256|HAMAP-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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}.
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DR   EMBL; CP001720; ACV61158.1; -; Genomic_DNA.
DR   RefSeq; WP_015755879.1; NC_013216.1.
DR   STRING; 485916.Dtox_0205; -.
DR   EnsemblBacteria; ACV61158; ACV61158; Dtox_0205.
DR   KEGG; dae:Dtox_0205; -.
DR   eggNOG; ENOG4105CAJ; Bacteria.
DR   eggNOG; COG1207; LUCA.
DR   HOGENOM; HOG000283476; -.
DR   KO; K04042; -.
DR   OMA; IEPQTHL; -.
DR   OrthoDB; 1381953at2; -.
DR   BioCyc; DACE485916:G1GFV-211-MONOMER; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002217; 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; C8W302.
DR   SWISS-2DPAGE; C8W302.
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   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458650};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01631,
KW   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   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458660};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458747}.
FT   DOMAIN        5    214       NTP_transferase. {ECO:0000259|Pfam:
FT                                PF00483}.
FT   REGION        1    229       Pyrophosphorylase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION        8     11       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       77     78       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      230    250       Linker. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   REGION      251    458       N-acetyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      385    386       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   ACT_SITE    362    362       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       102    102       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       227    227       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      22     22       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      72     72       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     139    139       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     154    154       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     169    169       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     227    227       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     332    332       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     350    350       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     365    365       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     376    376       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     379    379       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     404    404       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     422    422       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     439    439       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
SQ   SEQUENCE   458 AA;  48795 MW;  1C472437554F844B CRC64;
     MKLAAVVLAA GKGTRMKSKI PKVLHKVSGL PMISHVLHSV SKAGIEKKVV VVGYQGDQVA
     AQLGQDVNIA VQEEQLGTAH ALLSAESMLR DFSGHILVLC GDTPLIKPQT LKDLVSFHVD
     SASVATVLTA KLEDPTGYGR VIRDKAGSVA KIVEQKDASP VELNIQEINT GIYCFQSEFL
     FEALRHISPN NAQGEYYLTD IIQLYVSQGR LVSAIAVVDA AEIQGINDRV HLAAAESVLR
     RQMLDKLMLG GVTVIDPAST FIDQTVEIGT DTVILPYTCI EGNTVIGSDC IIGPHTRLSD
     TRIGNCVEIQ NSVLLKSDVG DQSSIGPFAY IRPDTVIGEQ VKVGDFVEIK KSNIGNKSKI
     PHLSYIGDSE IAENVNIGAG TITCNYDGVA KHRTTIEEGA FIGSNTNLVA PVSVGAGAVI
     GAGSTITMDV PPGALGVARG KQKNINNWLS RKTPEKRD
//

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