ID Q6FBY9_ACIAD Unreviewed; 517 AA.
AC Q6FBY9;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Putative acyl-CoA ligase {ECO:0000313|EMBL:CAG68422.1};
DE EC=6.2.1.- {ECO:0000313|EMBL:CAG68422.1};
GN OrderedLocusNames=ACIAD1572 {ECO:0000313|EMBL:CAG68422.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68422.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG68422.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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DR EMBL; CR543861; CAG68422.1; -; Genomic_DNA.
DR RefSeq; WP_004925140.1; NC_005966.1.
DR AlphaFoldDB; Q6FBY9; -.
DR STRING; 202950.GCA_001485005_02008; -.
DR GeneID; 45233963; -.
DR KEGG; aci:ACIAD1572; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_6; -.
DR OrthoDB; 9803968at2; -.
DR BioCyc; ASP62977:ACIAD_RS07210-MONOMER; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR24096:SF323; BLR3536 PROTEIN; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:CAG68422.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430}.
FT DOMAIN 6..357
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 416..494
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 145..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 57244 MW; F13F131EAC30B0C4 CRC64;
MHPMVHAQNT PDKAACIFAS TQQVLSYAQM NALANRCAHL FRQHGLKRGD VVSILLENSI
DIFTVAWAAQ RSGLYLTAIS CKTSAKDLAY ILDNSESKIL IVSECLVDTA LEALQLSQLD
YVYLYATGQK TSVASFTQAL SQCREDDITD PSPGGDMLYS SGSTGRPKGV RPPLPEGDLM
QPVPLMAMGR DLYQMNQDTL YLSTSPLYHA APLRWALAVH RFGGTVVIMD KYDAEQTLNL
IEQYQISHAT FVPTHFIRLL NLPETRRQSF DSSSLKAVIH AAAPCPVPVK QAMIDWWGPL
LHEYYSGTEQ CGITALDSVQ WLDKPGSVGK AVLGKIKVLD EQQNELAVGQ IGDIYFADGP
QFEYYKDPEK TKTAYSKQGW ATLGDIGWVD EDGYLYLTDR KNFMIISGGV NIYPQEIENL
LMTHPDVNDT AVFGIPDDEM GEKVVAIVQL KACILSSADE AQKLKQFVRQ ALGGVKCPQV
FEFCQNFPRE ATGKILKRKL IEDYKAHLAS STQAHSA
//
