(data stored in SCRATCH9089 zone)

SWISSPROT: GLMU_BURP1

ID   GLMU_BURP1              Reviewed;         453 AA.
AC   Q3JWX1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   11-DEC-2019, entry version 91.
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=BURPS1710b_0518;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) 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=ABA49097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000124; ABA49097.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004190034.1; NC_007434.1.
DR   SMR; Q3JWX1; -.
DR   EnsemblBacteria; ABA49097; ABA49097; BURPS1710b_0518.
DR   KEGG; bpm:BURPS1710b_0518; -.
DR   HOGENOM; HOG000283476; -.
DR   KO; K04042; -.
DR   OrthoDB; 1381953at2; -.
DR   BioCyc; BPSE320372:G1G58-578-MONOMER; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00113; UER00533.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002700; Chromosome I.
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; Q3JWX1.
DR   SWISS-2DPAGE; Q3JWX1.
KW   Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW   Peptidoglycan synthesis; Repeat; Transferase.
FT   CHAIN           1..453
FT                   /note="Bifunctional protein GlmU"
FT                   /id="PRO_0000233749"
FT   REGION          1..225
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          6..9
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          76..77
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          98..100
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          226..246
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          247..453
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          382..383
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   ACT_SITE        359
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   METAL           100
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   METAL           223
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         20
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         71
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         135
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         150
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         165
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         223
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         329
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         347
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         362
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         373
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         376
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         401
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         419
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
SQ   SEQUENCE   453 AA;  47580 MW;  D10729361F10D8CE CRC64;
     MNIVILAAGT GKRMRSALPK VLHPLAGRPL LSHVIDTARA LAPSRLVVVI GHGAEQVRAA
     VAAPDVQFAV QEQQLGTGHA VRQALPLLDP SQPTLVLYGD VPLTRTATLK RLADAATDAR
     YGVLTVTLDD PTGYGRIVRD QAGCVTRIVE QKDASPDELR IDEINTGIVV APTAQLSMWL
     GALGNDNAQG EYYLTDVVEQ AIEAGFEIVT TQPDDEWETL GVNSKAQLAE LERIHQRNLA
     DALLAAGVTL ADPARIDVRG TLACGRDVSI DVNCVFEGDV TLADGVTIGA NCVIRHAAIA
     AGARVDAFSH LDGATVGANA VVGPYARLRP GAVLAADAHV GNFVEVKNAT LGQGSKANHL
     TYLGDADIGA RVNVGAGTIT CNYDGANKFR TVIEDDVFVG SDTQFVAPVR VGRGVTVAAG
     TTVWKDVAAD MLVLNDKTQT AKSGYVRPVK KKS
//

If you have problems or comments...

PBIL Back to PBIL home page