(data stored in ACNUC7421 zone)

SWISSPROT: GLMU_HISS2

ID   GLMU_HISS2              Reviewed;         453 AA.
AC   B0UW09;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   11-DEC-2019, entry version 72.
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=HSM_0204;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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: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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACA31826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000947; ACA31826.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041604967.1; NC_010519.1.
DR   SMR; B0UW09; -.
DR   EnsemblBacteria; ACA31826; ACA31826; HSM_0204.
DR   GeneID; 31486482; -.
DR   KEGG; hsm:HSM_0204; -.
DR   HOGENOM; HOG000283476; -.
DR   KO; K04042; -.
DR   OrthoDB; 1381953at2; -.
DR   BioCyc; HSOM228400:G1GB8-209-MONOMER; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00113; UER00533.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000008543; 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; 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.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; B0UW09.
DR   SWISS-2DPAGE; B0UW09.
KW   Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW   Peptidoglycan synthesis; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..453
FT                   /note="Bifunctional protein GlmU"
FT                   /id="PRO_0000337723"
FT   REGION          1..227
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          9..12
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          79..80
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          101..103
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          228..248
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          249..453
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          384..385
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   ACT_SITE        361
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   METAL           103
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   METAL           225
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         23
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         74
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         138
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         152
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         167
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         225
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         331
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         349
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         364
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         375
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         378
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         403
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         421
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         438
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
SQ   SEQUENCE   453 AA;  49412 MW;  EEB8AE6E28EBA3AD CRC64;
     MNKLSVVILA AGKGTRMYSD LPKVLHKIAG KPMVKHVIDT AKKLSAAQIH LIYGHGADLL
     KQHLADEPVN WVFQSEQLGT GHAMQQAVPF FQDDENIVML YGDVPLISKE TLECLISQKP
     ENGIALLTVN LDNPTGYGRV IRENGTVTAI VEQKDANPEQ LKITEVNTGV MVSDGASFRK
     WLARLDNNNA QGEYYMTDVI GLANQDGFKV VAVQAKDLME VEGVNNRLQL ANLERHYQRK
     QVEKLLLAGV TFADPARFDL RGELTHGKDV EIDINVIIEG TVRLGNNVFI GAGCVLKNCT
     IADNVEIKPY SVIEDAIVGN NAKIGPFSRL RPGAELSENT HVGNFVEIKK AQIGKGSKVN
     HLTYIGDAEV GHHCNIGAGV ITCNYDGANK FKTLIGDNVF VGSDSQLVAP LTIASGATIG
     AGTTVTKDVQ ENELVITRVP QRHISNWQRP KRK
//

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