ID F6CUB6_MARPP Unreviewed; 565 AA.
AC F6CUB6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=Mar181_2197 {ECO:0000313|EMBL:AEF55235.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF55235.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF55235.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(2012).
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; CP002771; AEF55235.1; -; Genomic_DNA.
DR RefSeq; WP_013796710.1; NC_015559.1.
DR AlphaFoldDB; F6CUB6; -.
DR STRING; 491952.Mar181_2197; -.
DR KEGG; mpc:Mar181_2197; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_7_6; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000009230; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR CDD; cd05936; FC-FACS_FadD_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
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 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:AEF55235.1}.
FT DOMAIN 40..426
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 477..552
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 61641 MW; AEB57D4383479BE8 CRC64;
MTMDTSLDNN ADNEKVPGSY LPDSLNPNGY QGLTDVLALA VDKYSDLPAF TSVGRTITYR
ELNEKSDAFA AYLQNDTDLS PGDRIAIQLP NIIQYPIVLF GAMKAGLVVV NTNPLYTPKE
LEHQFNDAGV KALVLCANVA SNVEKILAKT SIKHVIITEI ADLHSPIKRV LVNSIVKYVK
KMVPAYDIPS ALSLNEVLAK GHGKPVSKVP VTPQHIAVLQ YTGGTTGVAK GAMLTNANLI
ANMYQLGSRL ESIVEERVET YIAPLPLYHI YAFLIHGLTL LQSGAHSVLI PNPRDLPGFV
SELKKWKFTG FVGLNTLFVG LCNRDDFRAL DFSNLKLTCS GGMPLTHAAA DEWKRMTGCQ
VVEGYGLTET SPVVSFNPIG EERIGTIGLP VGETDIKIQG DNGEALPQGE SGMLCVRGPQ
VMKGYWNREE ATREVMTEDG FLITGDIAMQ HEDGYLQIVD RAKDMIIVSG FNVYPTEVED
CISSHPAILE SAAIGVPDDK TGEAVKAYVV MKAGESIDIN ALRVFCKEHL AAYKVPKHIE
VRTELPKTNV GKVLRRALRE EEMAS
//
