ID A0A1F7Z1N1_9BACT Unreviewed; 411 AA.
AC A0A1F7Z1N1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Nucleotidyl transferase domain-containing protein {ECO:0000259|Pfam:PF00483};
GN ORFNames=A3D01_05220 {ECO:0000313|EMBL:OGM32625.1};
OS Candidatus Woesebacteria bacterium RIFCSPHIGHO2_02_FULL_39_13.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802505 {ECO:0000313|EMBL:OGM32625.1, ECO:0000313|Proteomes:UP000177169};
RN [1] {ECO:0000313|EMBL:OGM32625.1, ECO:0000313|Proteomes:UP000177169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGM32625.1}.
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DR EMBL; MGGR01000029; OGM32625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7Z1N1; -.
DR STRING; 1802505.A3D01_05220; -.
DR Proteomes; UP000177169; Unassembled WGS sequence.
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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..205
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 411 AA; 45484 MW; 5EE53108F4841BC9 CRC64;
MTRIFFPSQA VILAAGINSR FVPFNSRNYH KSNFLLMGEP IIRQTVGVLK KAGIKEVVVI
TSPKDKMTKK SLENLGGKGI GLDFYTQKQP LGMASALLGV KRYLHDKFLV INPQQINIDT
HLSRLKNIKT LSKNTVCLFS QSTDQPQKYG ILGLKGKRVT KVVEKPANLS GLSNQRILGV
YILNSDFMDL MGNFNITEYL LEEALNKYAS QGEVIAIRSD HPALSLKYAW DLFSIANYKF
SQFPQTPKVH KKAWVHPTAI ISGPVVIENG AKIYEYTLIQ GPCYIGKNCL VGSFCKIRKE
TVLEEDTELQ NSVEIKHSII GAKTHIHSGF IGDSIIGENC RIGAGFITAN RRLDRDNIRV
LIKDRLVDVG TSFGSVIGDN VKIGIHCGTN PGTVIASNSL VLPMTLISHQ K
//
