ID A5FXY5_ACICJ Unreviewed; 572 AA.
AC A5FXY5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00039545};
DE EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121};
DE AltName: Full=Long-chain acyl-CoA synthetase {ECO:0000256|ARBA:ARBA00042773};
GN OrderedLocusNames=Acry_1256 {ECO:0000313|EMBL:ABQ30467.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30467.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ30467.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30467.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; CP000697; ABQ30467.1; -; Genomic_DNA.
DR RefSeq; WP_011942105.1; NC_009484.1.
DR AlphaFoldDB; A5FXY5; -.
DR STRING; 349163.Acry_1256; -.
DR KEGG; acr:Acry_1256; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_9_5; -.
DR Proteomes; UP000000245; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05936; FC-FACS_FadD_like; 1.
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; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF8; 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:ABQ30467.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000245}.
FT DOMAIN 41..434
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 485..560
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 572 AA; 62994 MW; EFDD1485AC8DDBA5 CRC64;
MTDTMQDSVE TDGIWFASYR EGVPHDIGDE LARTPSLNHM LETWARTYAT REAFVSIGTP
MTYAETHARA RAFAGFLQAR GIAKGDRVAI MMPNSLQYPI AVFGTLLAGG TVVNVNPLYT
ARELNHQLRD SGAKLLVVFE NFARTAEQGL AGTAVETVVL TGIGDLLGGL KGPALNFVLR
HVQKAVPKHG LRARRFRAAL AEGRRAGLRP VELGHEDIAF LQYTGGTTGV AKGAMLTHRN
IIANVLQAFA WNGDQFHGEG VNNLTLLPLY HIFSLTVNLF MFMALGGRNV LIANPRDTKR
VMGIIRNEKF EGMAGINTLF NSFLDNEDFR RLDFSKLRLV IAGGAATQAE VAKRWQEVTG
RPISEGYGLT ECSPIVCTNP IDLDHPERMS FNGTVGLPLP STEVRLRRTD GAWAGIGEAG
EVCVRGPQVM RGYWQRPDET ARVLDAEGWL ATGDIGIMDE RGFLRLVDRA KDMILVSGFN
VYPSEIEEVV MMHPDVIEVA AFGVPDAASG ERVKIVVVPR SDTLTEAELL AHCRRNLTGY
KMPKIVEFRH EELPKTPVGK ILRRELRAQH DA
//
