ID B0SS93_LEPBP Unreviewed; 624 AA.
AC B0SS93;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Long-chain acyl-CoA synthetase, AMP-forming {ECO:0000313|EMBL:ABZ97983.1};
DE EC=6.2.1.3 {ECO:0000313|EMBL:ABZ97983.1};
GN OrderedLocusNames=LEPBI_I1879 {ECO:0000313|EMBL:ABZ97983.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97983.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ97983.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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DR EMBL; CP000786; ABZ97983.1; -; Genomic_DNA.
DR RefSeq; WP_012388861.1; NC_010602.1.
DR AlphaFoldDB; B0SS93; -.
DR STRING; 456481.LEPBI_I1879; -.
DR KEGG; lbi:LEPBI_I1879; -.
DR HOGENOM; CLU_000022_45_5_12; -.
DR OrthoDB; 311554at2; -.
DR BioCyc; LBIF456481:LEPBI_RS09280-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43813; ACYL-ACTIVATING ENZYME 16, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR43813:SF1; ACYL-ACTIVATING ENZYME 16, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ABZ97983.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT DOMAIN 34..455
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 624 AA; 70319 MW; D77B2C21A351132F CRC64;
MKNFTTLNDV FYYAKKNYGS KEMFFAKDTA KNFKGRTFSD IFHEAENLAL SLLQMGLQPG
DRIGLMADNR TEWAIADIAT LLNGAVNVPR GSDSTAQEIE YILSHSESKY CFVEHEKLYD
SLKPILSTTK VEKVIILDPT YVPKDSTVVN LQTLVRDGEA LRKNLPSLEL RSKQVKPDDL
FTIIYTSGTT GMPKGVMLTH QNMVYNVVKV PPRVGLKSTD RTLSILPVWH IFERAIDYAI
ITEGASIAYT NIRDLRDDFQ KIKPSFMASA PRLWENLYLG IKQKLEKAPE NKKKLFDFAY
DICKKFKDGQ DYLAGNRLLT KEESPFERMK NTTVSIGYVL NLFLLAKLLD GLVFSKIRDV
LGGHLTGTIS GGGALPSHVD EFFNVIGIPV YEGYGMTECA PIISVRSVGH VVQGSVGKWP
EGTAVRIVNE QGESVPKGKM GVIHIKGPQV MKGYYKNEEA TKKAIVDGWM NTGDLGFISF
NDTLSVRGRV KDTIVLLGGE NVEPVPIENL LLENALINQV IVVGQDQKSL TALVWPDKER
MKEVGLQWKE GEDLNQNKDV RLYYQNIVKK QISSENGFKS FEKLSDFRFL PKAMEVGDEL
TNLFKMKRNI IHDKYKDLIK SMYN
//
