ID   A0A087C0I9_9BIFI        Unreviewed;       705 AA.
AC   A0A087C0I9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Acyl-CoA synthetase {ECO:0000256|ARBA:ARBA00032875};
GN   ORFNames=BMON_0693 {ECO:0000313|EMBL:KFI76789.1};
OS   Bifidobacterium mongoliense DSM 21395.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI76789.1, ECO:0000313|Proteomes:UP000029082};
RN   [1] {ECO:0000313|EMBL:KFI76789.1, ECO:0000313|Proteomes:UP000029082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI76789.1,
RC   ECO:0000313|Proteomes:UP000029082};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFI76789.1}.
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DR   EMBL; JGZE01000011; KFI76789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087C0I9; -.
DR   STRING; 1437603.GCA_000771525_01115; -.
DR   eggNOG; COG1022; Bacteria.
DR   Proteomes; UP000029082; Unassembled WGS sequence.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   CDD; cd05907; VL_LC_FACS_like; 1.
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; PTHR43272:SF83; ACYL-COA SYNTHETASE LONG-CHAIN, ISOFORM J; 1.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 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:KFI76789.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029082}.
FT   DOMAIN          43..426
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   REGION          605..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   705 AA;  76575 MW;  28D774B4BC57BC4C CRC64;
     MREYAVDAVR TTTEKDTIYS LLSGRAARDG GDLIAQWLDE RRVWHDVTAD EMLGRVRAVA
     KGLMGLGVKP GSMVVIYSAT CYEWGVVDFA CAAIGAVSVP IYETDSARQA AGIVADVEPM
     VAFAGDDAHA QIFEGIRQHN TALKYVFNFR SGALDAVTDF GSSVGDDELD RAISRVSADD
     MATIVYTSGS TGKPKGAMLS HRNFTHIVFA GYDVLNEMLY QPSRLMLFLP LAHCFARYIQ
     YVAIGSHGVV GYVPNAGHLL ADMRSFRPTY LLGVPRVFEK VYNAASQKAG VGMKGRVFAN
     GFNHFVQWSK DEGAGKAHSV LDRIRHTFYM NAIGSSIRSA LGPNMRYLAC GGAPIDADLA
     HFFNGFDDIT FIQGYGMTET AAPCVVNFAK SNRVGSVGKP GPGIAIRLAD DDEVLIKGAN
     VFLGYYKQPD LTAEVLDADG WLSSGDLGRI DDDGFLYITG RKKDIIITAG GKNISPAPME
     NAIGNCPIVS HAVVLGDGRP FVSALVALDP DMAYSWLIQQ GMDGDMPMAR IAKNEAVRAF
     VQQYVDQANS RVSRAESVRK FIIVDKDFNL EDGTLTPSMK PVRPKILERY EELIDQVLYA
     PRGQARQPSA TVKILDRTSE TVKQASENVR QASETMSPKV RQALDQAKEY INKRAQDGRN
     GEVDEPAKAD ADHAGDAPSQ SSVPETRGAR DDGTCTTRRT PADGD
//