ID K2CZ66_9BACT Unreviewed; 414 AA.
AC K2CZ66;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:EKD90986.1};
GN ORFNames=ACD_30C00052G0004 {ECO:0000313|EMBL:EKD90986.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD90986.1};
RN [1] {ECO:0000313|EMBL:EKD90986.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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 -!- 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:EKD90986.1}.
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DR EMBL; AMFJ01011951; EKD90986.1; -; Genomic_DNA.
DR AlphaFoldDB; K2CZ66; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
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; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKD90986.1}.
FT DOMAIN 8..213
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 414 AA; 45724 MW; 3560A9899E2B68B9 CRC64;
MNKQSVEKVI VLAAGESSRF WPLATKVHKS FYKMGLGASL IEVTIFNLLK NIKQIKEIYI
VVSPKDKDRA VSLFLGNPKI KIVTQNLPKG QGDAILSAKE FISKDEKVFI TSADKINAYK
LFQSLQTREN ESIAVRTSDS ANLYGMVRLN INRRVVDVSE KPSKKGEYKL RITSGYILDS
RFFNYLDKVK KEHYSLEIAL KKYIKDVDVA GVLVDDIEEV TLKFAWHLLN INALLLSELK
GTHIAPSASI SPTAKIEGPV VIGAEAKVLD FAKISGPVYI GKNAVVGDYS SIRENSFIDD
EVLVGSHSEI KNSIIYKGGH LHRNYVGDSI IDEGTRIGAG TVFANRRIDR GEIQSKIKKI
KISTGLTSFG AILGRDVKLG VNCSLMPGVK IGEESMVLPQ TCVFDDIEDK GVTK
//
