ID   GLMU_META3              Reviewed;         411 AA.
AC   A6UUQ4;
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=Maeo_0642;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
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}.
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DR   EMBL; CP000743; ABR56226.1; -; Genomic_DNA.
DR   RefSeq; WP_011973358.1; NC_009635.1.
DR   AlphaFoldDB; A6UUQ4; -.
DR   SMR; A6UUQ4; -.
DR   STRING; 419665.Maeo_0642; -.
DR   EnsemblBacteria; ABR56226; ABR56226; Maeo_0642.
DR   GeneID; 5326905; -.
DR   KEGG; mae:Maeo_0642; -.
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; UP000001106; 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; 2.
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_0000337828"
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         132
FT                   /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57776"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
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;  45555 MW;  A02C8D6A6D815E8A CRC64;
     MDAVILCAGK GTRLMPLTEN IPKPMLPVGG APILERIINK IDKLVENIYL IVKYEKEIII
     NHFKNNDKIK FIEQTDIDGT GYAVLMAKNH ISGDFLVING DIIFDDDLTN IVNDDVKNII
     TLNEVDNPSN FGVIVVDNQN NIIELQEKPK NPKSNLINAG IYKFENKIFD ILETLRPSER
     GEVELTDAIK ELIKENNIKG IKLNGYWNDI GKPWDLLDAN THILKNIKTD IKGKIGKNVV
     IEGAVIIEEG TEIKPNTVIE GPAIIKSGAI VGPLAHIRPN TVLMENTGVG NSSEIKGSII
     MKNSKVPHLS YIGDSIIGEN CNMGCNTITA NLRFDNKPVM VNIKEEKVKS VRKFGAIIGH
     NVKTGIQVSF MPGVKIGSNS WIGANCLINN DIEKDSFVYK KEEIIIKTKR K