ID A0A0Q4RW30_9BURK Unreviewed; 618 AA.
AC A0A0Q4RW30;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Fatty-acid--CoA ligase {ECO:0000313|EMBL:KQO25469.1};
GN ORFNames=ASF16_21325 {ECO:0000313|EMBL:KQO25469.1};
OS Acidovorax sp. Leaf78.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736237 {ECO:0000313|EMBL:KQO25469.1, ECO:0000313|Proteomes:UP000051234};
RN [1] {ECO:0000313|Proteomes:UP000051234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
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:KQO25469.1}.
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DR EMBL; LMLZ01000005; KQO25469.1; -; Genomic_DNA.
DR RefSeq; WP_056163954.1; NZ_LMLZ01000005.1.
DR AlphaFoldDB; A0A0Q4RW30; -.
DR STRING; 1736237.ASF16_21325; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000051234; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05907; VL_LC_FACS_like; 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; 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:KQO25469.1}.
FT DOMAIN 46..446
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 618 AA; 68151 MW; 344C17582281EE64 CRC64;
MSNLWDLDHI QPAGTDVLAG STISAMFWNA VALRGPNVWM RQKELGIWKS WTWDQTAEAV
REIAGGLMAL GFARGDCASI LSNTNIEWVL ADLAVLSCGG VSNGIYPTDA AAQVHYLSED
SATTVLFVEN DEQLDKALEV RAGLPLLRRI IVFDMEGLRG LQDPGVISLQ ALRDLGRAWN
QQNPDALMRR VQACQPEDVA ILVYTSGTTG KPKGAMHTHA ALVYTVRGYN TLISRTDQDE
AMCFLPLCHI AERMGGEYFS LYTGSRLNFV ENPDTVPENV REIAPTVFTA VPRVWEKFYS
GVMIALKEST ALQQAAYAWS IGVGTRIADL VLAGQPVGGL LKLQFQLARW LALNNVRKLI
GIHRARFLVT GAAPISPELV KWYLALGVPM LEVWGMTETC GAATGVPASR IKPGSIGPAA
AYNEVRIDPA TGEILVRGPN VFKGYLNLPE KTAETIDADG WLHTGDVGTI DADGYLRITD
RMKDIIITAG GKNITPSELE NELKFSPYVT DAVVIGDKLP YLTVIIMIDQ ENVEKFAQDN
DVPFSNYASL TRAREVQDLI QAEIDRVNTQ FARVEQIKKF FLLDTQLTAE DEELTPTMKL
KRKLVQQKYA AQIEAMYR
//
