GLMU_METVS
ID GLMU_METVS Reviewed; 414 AA.
AC A6UP85;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Bifunctional protein GlmU;
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;
DE EC=2.7.7.23;
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase;
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase;
DE EC=2.3.1.157;
GN OrderedLocusNames=Mevan_0399;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo
CC biosynthetic pathway for UDP-N-acetyl-glucosamine (UDP-GlcNAc).
CC Responsible for the acetylation of GlcN-1-P to GlcNAc-1-P, and for the
CC uridyl transfer from UTP to GlcNAc-1-P, to produce UDP-GlcNAc and
CC pyrophosphate (By similarity). {ECO:0000250}.
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 -!- 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 -!- 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 -!- 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 -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000742; ABR54307.1; -; Genomic_DNA.
DR RefSeq; WP_011972210.1; NC_009634.1.
DR AlphaFoldDB; A6UP85; -.
DR SMR; A6UP85; -.
DR STRING; 406327.Mevan_0399; -.
DR EnsemblBacteria; ABR54307; ABR54307; Mevan_0399.
DR GeneID; 5325640; -.
DR KEGG; mvn:Mevan_0399; -.
DR eggNOG; arCOG00666; Archaea.
DR HOGENOM; CLU_029499_0_1_2; -.
DR OMA; TAIVEHK; -.
DR OrthoDB; 61185at2157; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR Proteomes; UP000001107; Chromosome.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR023915; Bifunctiontional_GlmU_arc-type.
DR InterPro; IPR001451; Hexapep.
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; TIGR03992; Arch_glmU; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Multifunctional enzyme; Nucleotidyltransferase; Repeat;
KW Transferase.
FT CHAIN 1..414
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000337832"
FT REGION 1..208
FT /note="Pyrophosphorylase"
FT REGION 209..228
FT /note="Linker"
FT REGION 229..414
FT /note="N-acetyltransferase"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 6..9
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
SQ SEQUENCE 414 AA; 45989 MW; B4BA852E48C77BC4 CRC64;
MDAVILCAGS GTRLYPITEN RPKPMIPIAG KPILEHIIEK IENHVEKIYL VVGFEKEKII
DYFYGNEKIE FIVQEKQLGT GHAVLMAKNY IKGDFLVLNG DVIFESDILE FLNYENAVGL
SKVDNPENFG VIELGYDNKV INLLEKPNED EIKSKFTSNL INAGIYKLEN FVFEILENLL
PSERGEIELT DALKKLIESS KLYGIELNGY WNDIGRPWDV LSANNYFLKN IMPKISGNIE
NNVTITGNVI IEEGVTVKSN SVIEGPVIIK SGAFIGPLAY IRPNTVLMED TFVGNSSEIK
GSIIMKNTKI PHLSYVGDSI IGSDCNFGCN TITANLRFDD EPVTLNIKGT KVKSVRKFGA
VIGDNVKTGI QVSLMPGVKV GSNSIIGANC LVDKDIEKES FVYKKDELII KKRN
