ID A7NQ86_ROSCS Unreviewed; 457 AA.
AC A7NQ86;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:ABU59732.1};
GN OrderedLocusNames=Rcas_3684 {ECO:0000313|EMBL:ABU59732.1};
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU59732.1, ECO:0000313|Proteomes:UP000000263};
RN [1] {ECO:0000313|EMBL:ABU59732.1, ECO:0000313|Proteomes:UP000000263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) 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};
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DR EMBL; CP000804; ABU59732.1; -; Genomic_DNA.
DR RefSeq; WP_012122155.1; NC_009767.1.
DR AlphaFoldDB; A7NQ86; -.
DR STRING; 383372.Rcas_3684; -.
DR KEGG; rca:Rcas_3684; -.
DR eggNOG; COG0110; Bacteria.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_607940_0_0_0; -.
DR OrthoDB; 9813880at2; -.
DR Proteomes; UP000000263; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
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; PF12804; NTP_transf_3; 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 Reference proteome {ECO:0000313|Proteomes:UP000000263};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABU59732.1}.
FT DOMAIN 5..131
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
SQ SEQUENCE 457 AA; 48746 MW; 24772F3526203ADB CRC64;
MIRTAILLAA GAGVRFWPYN VVRNKCAFPI ANVPAIRRLS DDLAALGVTR QVVVVGAGEA
SIRAALRGAA AEIVFARQAR PDGTAAAALL GAASIDDDLL VVAGDIVTDR ANLAALRDRF
ERDRPLAAAL VQPLGAESSL DWLIPFVDNG VLHGVEGHSR DGDRRFCGVY AFRPEALPFL
RDNPALVRVG VGGMPPVDAE IVQSLQMMVD EGERVATVDA PGFHVDLDKP WHILEANARV
IDAMAAALDG DRIDPTARVH DGADIRGRLI LGPGAEIGNR AVVEGDLWLG AGAKALNGAI
IQGRAVVGRE TVLRDYCLIG AHSSLGARGI YGHGAEFSGV ALDTVYCYHY CEIWGVVGMA
VDFGAATVCG NLRFDDRATV WRINGRPEIP TTAANAAYFG DFCRTGVNAI IMPGRRLGAY
SICGPGVILR DDLPDRAMVM VEQQVTTRPW GPERYGW
//
