ID A0A062V9E6_9EURY Unreviewed; 403 AA.
AC A0A062V9E6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|ARBA:ARBA00013414};
DE EC=2.3.1.157 {ECO:0000256|ARBA:ARBA00012225};
DE EC=2.7.7.23 {ECO:0000256|ARBA:ARBA00012457};
GN ORFNames=ANME2D_00238 {ECO:0000313|EMBL:KCZ73178.1};
OS Candidatus Methanoperedens nitroreducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1392998 {ECO:0000313|EMBL:KCZ73178.1, ECO:0000313|Proteomes:UP000027153};
RN [1] {ECO:0000313|EMBL:KCZ73178.1, ECO:0000313|Proteomes:UP000027153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANME-2d {ECO:0000313|EMBL:KCZ73178.1,
RC ECO:0000313|Proteomes:UP000027153};
RX PubMed=23892779; DOI=10.1038/nature12375;
RA Haroon M.F., Hu S., Shi Y., Imelfort M., Keller J., Hugenholtz P., Yuan Z.,
RA Tyson G.W.;
RT "Anaerobic oxidation of methane coupled to nitrate reduction in a novel
RT archaeal lineage.";
RL Nature 500:567-570(2013).
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. {ECO:0000256|ARBA:ARBA00024726}.
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 Evidence={ECO:0000256|ARBA:ARBA00001851};
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 Evidence={ECO:0000256|ARBA:ARBA00000731};
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 {ECO:0000256|ARBA:ARBA00005166}.
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 {ECO:0000256|ARBA:ARBA00005208}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007947}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KCZ73178.1}.
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DR EMBL; JMIY01000001; KCZ73178.1; -; Genomic_DNA.
DR RefSeq; WP_048088408.1; NZ_JMIY01000001.1.
DR AlphaFoldDB; A0A062V9E6; -.
DR PATRIC; fig|1392998.3.peg.601; -.
DR OrthoDB; 15372at2157; -.
DR UniPathway; UPA00113; UER00532.
DR Proteomes; UP000027153; Unassembled WGS sequence.
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 CDD; cd05636; LbH_G1P_TT_C_like; 1.
DR CDD; cd04181; NTP_transferase; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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 NCBIfam; TIGR03992; Arch_glmU; 1.
DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:KCZ73178.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KCZ73178.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027153};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KCZ73178.1}.
FT DOMAIN 2..228
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 403 AA; 43526 MW; 2F41DDAB9DF582BD CRC64;
MKAVILAAGK GTRMGPLTES RPKVMLPIDN RPILEHIIVR LKAAGIKDFL VVIGYCKEKI
TDYFGDGSML GVGIEYIEQQ NPKGTADAIA TARDSIDERF LVTNGDVLAD PSDIKKIISA
GGDAVLAAKR VAVPEEYGIL YVKGNKVEKI VEKPKESTSD LANAGIYVFE PVIFNAIDNT
NPSPRGEYEI TDSIQFMIDR GNELSCAALE RWQDIGFPWH LLTANEIALN EREDWDIQGE
IEPYVTLKGK VAVGKGTVIR SGAYITGPVV IGENCDIGPN CFIRPGTSIA DNVRIGNAVE
VKNSIVMSGT NIGHLSYVGD SIIGEKCNFG AGTKVANLRH DNRTVMVELG GRRFNSGRRK
LGVIMGDDVH TGINSMINVG TTIASGAFID PGEFIKGTYP ANR
//
