ID Q72B05_DESVH Unreviewed; 304 AA.
AC Q72B05;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Biotin--acetyl-CoA-carboxylase ligase {ECO:0000313|EMBL:AAS96311.1};
GN OrderedLocusNames=DVU_1835 {ECO:0000313|EMBL:AAS96311.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS96311.1, ECO:0000313|Proteomes:UP000002194};
RN [1] {ECO:0000313|EMBL:AAS96311.1, ECO:0000313|Proteomes:UP000002194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000313|Proteomes:UP000002194};
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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DR EMBL; AE017285; AAS96311.1; -; Genomic_DNA.
DR AlphaFoldDB; Q72B05; -.
DR SMR; Q72B05; -.
DR STRING; 882.DVU_1835; -.
DR PaxDb; 882-DVU_1835; -.
DR EnsemblBacteria; AAS96311; AAS96311; DVU_1835.
DR KEGG; dvu:DVU_1835; -.
DR eggNOG; COG0340; Bacteria.
DR HOGENOM; CLU_051096_1_0_7; -.
DR PhylomeDB; Q72B05; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR NCBIfam; TIGR00121; birA_ligase; 1.
DR PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AAS96311.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002194}.
FT DOMAIN 62..238
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 304 AA; 32119 MW; F026BA239132E9F8 CRC64;
MLTAGLADVA APLSLDELDR SGFLGPLFES FGCPAGAQPR AFSAGQGVGC SHDGEWDVLE
LAAGNETLFL CGDATSSLDV ARILTDRGAL PEWGMVLVLS QSAGRGQLRR PWVSPRGNVY
AALRLPADPP FTADYAALSV GCMLAEGFRT LGIPVQLKWP NDILLDDCKV GGILLEERAG
IIIAGIGINC TFAPPVAQLR DGWAVRAASL LEKGYDLTPL ALFASLVKNG RFWYLNEIRR
AGHGAFPSCA ERHLAWMGRG IVVHGGDVDD KPGRIAGLSS EGGLRVRFPD GERVILSGSI
VPGS
//
