(data stored in SCRATCH zone)

SWISSPROT: D3VG26_XENNA

ID   D3VG26_XENNA            Unreviewed;       462 AA.
AC   D3VG26;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
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   ECO:0000313|EMBL:CBJ88116.1};
GN   OrderedLocusNames=XNC1_0023 {ECO:0000313|EMBL:CBJ88116.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88116.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88116.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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}.
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DR   EMBL; FN667742; CBJ88116.1; -; Genomic_DNA.
DR   RefSeq; WP_013183043.1; NC_014228.1.
DR   STRING; 406817.XNC1_0023; -.
DR   EnsemblBacteria; CBJ88116; CBJ88116; XNC1_0023.
DR   KEGG; xne:XNC1_0023; -.
DR   eggNOG; ENOG4105CAJ; Bacteria.
DR   eggNOG; COG1207; LUCA.
DR   HOGENOM; HOG000283476; -.
DR   KO; K04042; -.
DR   OMA; IEPQTHL; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000008075; 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; 3.
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; D3VG26.
DR   SWISS-2DPAGE; D3VG26.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458646, ECO:0000313|EMBL:CBJ88116.1};
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:UP000008075};
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, ECO:0000313|EMBL:CBJ88116.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458685};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
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, ECO:0000313|EMBL:CBJ88116.1}.
FT   DOMAIN       13    127       NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
FT   REGION        1    234       Pyrophosphorylase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       16     19       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       86     87       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      108    110       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      235    255       Linker. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   REGION      256    462       N-acetyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      391    392       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   ACT_SITE    368    368       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       110    110       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       232    232       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      30     30       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      81     81       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     145    145       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     159    159       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     174    174       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     232    232       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     338    338       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     356    356       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     371    371       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     382    382       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     385    385       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     410    410       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     428    428       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     445    445       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
SQ   SEQUENCE   462 AA;  49818 MW;  2F98BC3A59A0A189 CRC64;
     MSIISNGVNT KSVVILAAGK GTRMYSDLPK VLHLLAGKPM VQHVIDTAME LGTQNVHLVY
     GHGGDLMKQT LSNQNLNWVL QAEQLGTGHA MQQAAPHFAD DEDILILYGD VPLIAKDTLA
     RLIEAKPEGG IGLLTAILDN PTGYGRIIRE NGDVTGIIEQ KDATEEQRKI NEINTGILVA
     NGGDLKRWLA KLENNNAQGE YYLTDVIALA YKEGCQIKAV HPSRLSEMEG VNNRLQLSAL
     ERIYQSEQAE KLLLAGVMLL DPARFDLRGT LVHGRDIVID TNVIIEGHVT LGNHVHIGSG
     CILKNCVIGD GAVISPYTVI EDSELSTECT VGPFARLRLG TKLAEQAHVG NFVEMKKASL
     GKGSKAGHLT YLGDAVIGDN VNIGAGTITC NYDGANKFKT IIGDDVFVGS DTQFVAPVTI
     EKGATIGAGT TVTKNVAENE LVISRVKQTH IKNWQRPVKK NK
//

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