ID   GLMU_METM5              Reviewed;         411 AA.
AC   A4FX98;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=MmarC5_0513;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-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}.
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DR   EMBL; CP000609; ABO34827.1; -; Genomic_DNA.
DR   RefSeq; WP_011868282.1; NC_009135.1.
DR   AlphaFoldDB; A4FX98; -.
DR   SMR; A4FX98; -.
DR   STRING; 402880.MmarC5_0513; -.
DR   EnsemblBacteria; ABO34827; ABO34827; MmarC5_0513.
DR   GeneID; 4927754; -.
DR   KEGG; mmq:MmarC5_0513; -.
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; UP000000253; 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..411
FT                   /note="Bifunctional protein GlmU"
FT                   /id="PRO_0000337829"
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;  45344 MW;  97A41672A49EC28C CRC64;
     MDAIILCAGK GTRLHPITES RPKPMIPIAG KPILEHIIEK IENHVEKIYL VVGFEKEKII
     EYFNENPKIE YILQEKQLGT GHAVLTAKNF IKDDFLVLNG DVIFEDSIDE ILDYENAVAL
     SKVDNPENFG VIELGYDNKV INLLEKPKKE ELTSNFINAG IYKLQNSVFG ILENLVPSER
     GEIELTDALK KLIEIGKLHG VELNGYWNDI GHPWDVLSAN SHFLNKIISK ISGKIENNVS
     ITGNVIIEEG AVIKSNSVIE GPVIIKSGSI VGPLAYIRPN TILMENNFVG NSSEIKGSII
     FENTKIPHLS YVGDSIIGAN CNFGCNTITA NLRFDNKPVI VNIKGKPVKS VRKLGAIIGD
     NVKSGIQVSF MPGVKIGSNS LIGANCLIDS DIEQESFVYK KDELVITKKR N