GLMU_METM7
ID GLMU_METM7 Reviewed; 411 AA.
AC A6VG23;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=MmarC7_0329;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
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; CP000745; ABR65399.1; -; Genomic_DNA.
DR RefSeq; WP_011976734.1; NC_009637.1.
DR AlphaFoldDB; A6VG23; -.
DR SMR; A6VG23; -.
DR STRING; 426368.MmarC7_0329; -.
DR EnsemblBacteria; ABR65399; ABR65399; MmarC7_0329.
DR GeneID; 5328824; -.
DR KEGG; mmz:MmarC7_0329; -.
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 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..411
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000337830"
FT REGION 1..204
FT /note="Pyrophosphorylase"
FT REGION 205..224
FT /note="Linker"
FT REGION 225..411
FT /note="N-acetyltransferase"
FT ACT_SITE 308
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 158
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
SQ SEQUENCE 411 AA; 45462 MW; 4233C9E0064CDC31 CRC64;
MDAIILCAGK GTRLYPITES RPKPMIPIAG KPILEHIIEK IENYVEKIYL VVGFEKEKII
EYFKENPKIE YILQEKQLGT GHAVLTAKNF IKDDFLVLNG DIIFEDSIDE ILVYENAVAL
SKVGHPENFG VVELGYDNKI INLLEKPKKE ELPSNLINAG IYKLQNNVFD ILENLVPSER
GEIELTDALK KLIENGKLHG IELNGYWNDI GHPWDVLSAN NRFLNKIISK VSGKIENNVS
ITGNVIIEEG AVIKPNSVIE GPVIIKSGSI VGPLAYIRPN TVLMENTFVG NSSEIKGSII
LENTKIPHLS YVGDSIIGAN CNFGCNTITA NLRFDDKPVM VNIKGKPVKS VRKLGAIIGD
NVKTGIQVSF MPGVKIGSNS LIGANCLIDN DIEQNSFVYK KDELVITKKR N
