ID A0A1B1EAV2_VIBNA Unreviewed; 563 AA.
AC A0A1B1EAV2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=BA894_04745 {ECO:0000313|EMBL:ANQ25795.1};
OS Vibrio natriegens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=691 {ECO:0000313|EMBL:ANQ25795.1, ECO:0000313|Proteomes:UP000092577};
RN [1] {ECO:0000313|EMBL:ANQ25795.1, ECO:0000313|Proteomes:UP000092577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 16374 {ECO:0000313|EMBL:ANQ25795.1,
RC ECO:0000313|Proteomes:UP000092577};
RA Weinstock M.T., Hesek E.D., Wilson C.M., Gibson D.G.;
RT "Developing Vibrio natriegens as a novel, fast-growing host for
RT biotechnology.";
RL Submitted (JUL-2016) 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; CP016351; ANQ25795.1; -; Genomic_DNA.
DR RefSeq; WP_020336111.1; NZ_JAPQMX010000002.1.
DR AlphaFoldDB; A0A1B1EAV2; -.
DR STRING; 691.BA893_04490; -.
DR GeneID; 70912967; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000092577; Chromosome 1.
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:ANQ25795.1}.
FT DOMAIN 29..419
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 470..544
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 563 AA; 62534 MW; 89FF961BD0F92276 CRC64;
MDKPWLSRYP SDVPETINPD QYESLVEMFE QSVQKYADQP AFMNMGSVMT FRKLEERSRA
FAAYLQNELK LKKGDRVALM MPNLLQYPVA LFGILRAGCI AVNVNPLYTP RELEHQLNDS
GATAIVIVSN FANTLEQIVE NTSVKHVVLT SLGQMLPRAK GTIVDFVVKY VKGMVPKYNL
PGAISMRKAL GKGRRLQYVK PFMSGDDIAF LQYTGGTTGV AKGAILTHRN MIANVLQAKG
AYGPVLTPGR ELVVTALPLY HVFALTVNCL LFIEMGGRNL LITNPRDIPG FVKELQKHPF
TAITGVNTLF NALVNNEDFH ELDFSNLRLS VGGGMAVQRA VAEKWLKTTG CYLLEGYGLT
ECSPLVAAYP HDLIEYNGSI GLPVPSTEVR IVDEEGNALP NTETGELQVR GPQVMQGYWQ
RPEASKDTIN QEGWLSTGDI VKFDDEGFLH IVDRKKDMIL VSGFNVYPNE IEDVVALHGK
VLEVAAIGQP NDVSGELVKI YVVKRDPSLT KDEVIAHCRE HLTGYKVPKL VEFREELPKT
NVGKILRRVL REENDAELAK KSA
//
