ID G0LMD8_HALWC Unreviewed; 399 AA.
AC G0LMD8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=graD3 {ECO:0000313|EMBL:CCC41258.1};
GN OrderedLocusNames=Hqrw_3501 {ECO:0000313|EMBL:CCC41258.1};
OS Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC41258.1, ECO:0000313|Proteomes:UP000007954};
RN [1] {ECO:0000313|EMBL:CCC41258.1, ECO:0000313|Proteomes:UP000007954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16854 / JCM 12705 / C23
RC {ECO:0000313|Proteomes:UP000007954};
RX PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA Rampp M., Oesterhelt D.;
RT "Haloquadratum walsbyi: limited diversity in a global pond.";
RL PLoS ONE 6:E20968-E20968(2011).
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 -!- 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}.
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DR EMBL; FR746099; CCC41258.1; -; Genomic_DNA.
DR RefSeq; WP_014556672.1; NC_017459.1.
DR AlphaFoldDB; G0LMD8; -.
DR GeneID; 12448320; -.
DR KEGG; hwc:Hqrw_3501; -.
DR HOGENOM; CLU_029499_0_1_2; -.
DR OrthoDB; 15372at2157; -.
DR Proteomes; UP000007954; Chromosome.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:RHEA.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:RHEA.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd04181; NTP_transferase; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:CCC41258.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCC41258.1}.
FT DOMAIN 6..231
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 399 AA; 42404 MW; CC804AB732D5AD1E CRC64;
MTIDTAVILA AGEGTRLRPL TTHRPKPMLP AGDIPILEHV LNSLVEAGIS EIHLVVGYQR
ARVQNHFGST YRNRPITYHI QHTQLGSGHA LLQADETIET DFLVLNGDQI VTEEMIETVS
SSHTATDTAT LGVVESEKAS QYGAVELNDN RITEFIEQPA DDEYRLLNAG VYVFGPSIFA
ALERTFQEQG RLSLPETIRD LTTDESAVRG VVTESPWQDA TYPWDLLSVM QTLFDQDRIG
DETTEQSPGV FSDQTATIHE DATLRPPVIV SADTVVGPQA VLGPGVAVGE NTTIGAGAVL
TNVLVDSDTR VGQNATLIDT VLGQGVHLGP GVIIAGGPAD IRIDTKVHED CDLGGVIADR
ATVGGGVTVA SGSLVGSAAT IQSNAHIDGN IPNEAEVLR
//
