ID A0A0G9MM46_9SPHN Unreviewed; 579 AA.
AC A0A0G9MM46;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:KLE31806.1};
DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:APE27823.1};
DE EC=6.2.1.3 {ECO:0000313|EMBL:APE27823.1};
GN ORFNames=AAW01_09945 {ECO:0000313|EMBL:KLE31806.1}, BMF35_a0994
GN {ECO:0000313|EMBL:APE27823.1};
OS Aurantiacibacter gangjinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=502682 {ECO:0000313|EMBL:KLE31806.1, ECO:0000313|Proteomes:UP000053070};
RN [1] {ECO:0000313|EMBL:KLE31806.1, ECO:0000313|Proteomes:UP000053070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K7-2 {ECO:0000313|EMBL:KLE31806.1,
RC ECO:0000313|Proteomes:UP000053070};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacr gangjinensis K7-2.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APE27823.1, ECO:0000313|Proteomes:UP000183202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC1.15024 {ECO:0000313|EMBL:APE27823.1,
RC ECO:0000313|Proteomes:UP000183202};
RA Xu L., Wu Y.-H., Cheng H., Zhou Y.-G., Wu M., Cheng L., Xu X.-W.;
RT "Complete genome sequence of two-chromosomal Erythrobacter gangjinensis
RT CGMCC 1.15024T, isolated from seawater.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP018097; APE27823.1; -; Genomic_DNA.
DR EMBL; LBHC01000002; KLE31806.1; -; Genomic_DNA.
DR RefSeq; WP_047007156.1; NZ_LBHC01000002.1.
DR AlphaFoldDB; A0A0G9MM46; -.
DR STRING; 502682.BMF35_a0994; -.
DR KEGG; egn:BMF35_a0994; -.
DR PATRIC; fig|502682.8.peg.2031; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000053070; Unassembled WGS sequence.
DR Proteomes; UP000183202; Chromosome i.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR CDD; cd05931; FAAL; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR040097; FAAL/FAAC.
DR PANTHER; PTHR22754:SF32; DISCO-INTERACTING PROTEIN 2; 1.
DR PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:APE27823.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053070}.
FT DOMAIN 52..428
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 579 AA; 63964 MW; 70360B76873FEFF3 CRC64;
MTETTSDLVP TPSDCSLPRI RSDFRTFTEA MDYAARSEKG MNFHDMRGTL EKVYSYTQMR
EDALGHARRL IGLGVEKGDR IALIAETAPE FTAMFAACVY AGAWPVPLPL PTTFGGKDSY
IDQLGVQLSS SDPKMLLYPA EIAEMAKAAA DKQGCAGYTW DEFAAHDAPD VDLPEASPQD
ICYLQYSSGS TRFPTGVAVT HEALLHNLYG HATSMDMRDG DRGVSWLPFY HDMGLVGCFL
SMVGNQMSAD YLRTEHFARR PLAWLDLISR NKGSTISYSP TFGYDICARR ISSQSHVADR
FDLSRWRLAG NGADMIRPDV MQQFVNAFAD AGFKASAFTP SYGLAEATLA VTVMPMGEGI
RVELVEEERL SGTKRDLSRP ARYRAIVNCG KPMPDLDVEI RGENGEVKGD HQIGKVWCRG
PSVMHSYFRD PQATEDCLVD GWLDTGDMGY MADGYLFIVG RAKDMIIING KNHWPQDIEW
AVEQLPGFNH GDIAAFALET DNGEEAPAVL VHCRVSDPDE RLKLRDQIAD KVRSVTGMNC
VVELVPPRTL PRTSSGKLSR AKAKKMYISG EIEPLQVAA
//
