ID A0A166DMK3_9EURY Unreviewed; 425 AA.
AC A0A166DMK3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 Name=glmU_3 {ECO:0000313|EMBL:KZX15761.1};
GN ORFNames=MBCUT_12640 {ECO:0000313|EMBL:KZX15761.1};
OS Methanobrevibacter cuticularis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX15761.1, ECO:0000313|Proteomes:UP000077275};
RN [1] {ECO:0000313|EMBL:KZX15761.1, ECO:0000313|Proteomes:UP000077275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX15761.1,
RC ECO:0000313|Proteomes:UP000077275};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZX15761.1}.
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DR EMBL; LWMW01000108; KZX15761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166DMK3; -.
DR STRING; 47311.MBCUT_12640; -.
DR PATRIC; fig|47311.3.peg.1385; -.
DR UniPathway; UPA00113; UER00532.
DR Proteomes; UP000077275; 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; 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; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000077275};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..236
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 425 AA; 47186 MW; C5D4895738C035F6 CRC64;
MKAIILSAGE GTRMRPLTLT KPKTMLPVAG KPIIQYNIEA LKDSGITDIL LIVKYKEEMV
KDYFKDGNDF GVNISYKTQE ELVGTANAIG YGQDFVDDTF IVLNGDIILD NELLTDIIKE
YSKFKVDTLM VLTEVENPSN FGVVEIENDL IKNIVEKPKK GEAPSNLVNT GIYIFNRDIF
SKIAKTNKSS RGEYEITDSL SMQIQDNKVV RGFKTDKKWI DVGRPWELIE INELLLSRIK
TNIKGKIENG AHIHGEIFLD EGSIIRSGVY IEGSVYIGKN CDIGPNCYIR GNSYFGDNVN
VGNAVEIKNS LIMENTNINH LSYVGDSVIG SNCNIAAGTN VANLRFDNDT VKTTIKNQKI
DSGRRKFGTI LGDSVQTGIN SSFSPGVKVG HNSSIGSDVL LYNDVDHNKV VLVKQKHIIF
DKEEK
//
