ID   GLMU_METMP              Reviewed;         411 AA.
AC   Q6LYB5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=MMP1076;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF30632.1; -; Genomic_DNA.
DR   RefSeq; WP_011171020.1; NC_005791.1.
DR   AlphaFoldDB; Q6LYB5; -.
DR   SMR; Q6LYB5; -.
DR   STRING; 267377.MMP1076; -.
DR   EnsemblBacteria; CAF30632; CAF30632; MMP1076.
DR   GeneID; 2761822; -.
DR   KEGG; mmp:MMP1076; -.
DR   PATRIC; fig|267377.15.peg.1109; -.
DR   eggNOG; arCOG00666; Archaea.
DR   HOGENOM; CLU_029499_0_1_2; -.
DR   OMA; TAIVEHK; -.
DR   OrthoDB; 61185at2157; -.
DR   BioCyc; MMAR267377:MMP_RS05565-MON; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00113; UER00533.
DR   Proteomes; UP000000590; 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;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..411
FT                   /note="Bifunctional protein GlmU"
FT                   /id="PRO_0000337831"
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;  45282 MW;  4C82577A9BB75E8B CRC64;
     MDAIILCAGK GTRLHPITES RPKPMIPIAG KPIIEHIIEK IENHVEKIYL IVGYQKEKII
     DYFKDNPKIE YILQEKQLGT GHAVLTAKNF IKGDFLVLNG DVIFEDSIDE ILNYENAVSL
     SNVDNPENFG VIELGYDNKI INLLEKPKKE EITSNLINAG IYKLQNSVFG ILENLAPSER
     GEIELTDALK KLIENGKLHG VELKGYWNDI GHPWDVLSAN NHFLNKIISK VSGKIENTVS
     ITGNVIIEEG AVIKPNSVIE GPAIIKSGSI VGPLAYVRPN TVLMKNTFVG NSSEIKGSII
     FENTKIPHLS YVGDSIIGAN CNFGCNTITA NLRFDDKPVI VNIKGKPVKS VRKLGAIIGD
     CVKTGIQVSF MPGVKIGSNS LIGANCLIDR DIEQESFVYK KDELVITKKR N