ID A9WD49_CHLAA Unreviewed; 390 AA.
AC A9WD49;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:ABY35016.1};
GN OrderedLocusNames=Caur_1799 {ECO:0000313|EMBL:ABY35016.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY35016.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY35016.1; -; Genomic_DNA.
DR RefSeq; WP_012257670.1; NC_010175.1.
DR RefSeq; YP_001635405.1; NC_010175.1.
DR AlphaFoldDB; A9WD49; -.
DR STRING; 324602.Caur_1799; -.
DR EnsemblBacteria; ABY35016; ABY35016; Caur_1799.
DR KEGG; cau:Caur_1799; -.
DR PATRIC; fig|324602.8.peg.2052; -.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_029499_0_1_0; -.
DR InParanoid; A9WD49; -.
DR Proteomes; UP000002008; Chromosome.
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 CDD; cd04181; NTP_transferase; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR018357; Hexapep_transf_CS.
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.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 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:UP000002008};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABY35016.1}.
FT DOMAIN 7..225
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 390 AA; 40982 MW; 2F721E39F7E8B76B CRC64;
MSSAKHAVIL VAGASTRTRP LTDQRPKPLI PLLGKPLLAH ILDELVGLVE RVTLVVGYRA
DQIVATFGET YRGMAIRYVY QTTINGTAGA LLAAAPIDEP FFLLYGDNLI DRADVIGVGQ
FRYALAGLRL PDLRSFGVLD VHDGLVQRII EKPTQPPPDA LANPGIYHFD AEVFPLLHRI
TPSPRGELEL TDLIALLAEQ HPVACHVCTG HWLPVGTPWE ALLAARFLLA RQAHTQPLPQ
IAPNAHIAPQ ADLEGSVVVS DGASIDQGAR IVGPAWIGPG AVIGSGALII ASVIEAGATI
GAEAMIGGSV IGAQTAVGAQ ASISHSWLDE RVQIGYQAVC QAAEYRDAPV NVVVNGLLTE
DDLITRGVVV AAGVAIAPQS VIAAGSIVRL
//
