ID C1A2A6_RHOE4 Unreviewed; 597 AA.
AC C1A2A6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Probable long-chain fatty-acid--CoA ligase {ECO:0000313|EMBL:BAH34741.1};
DE EC=6.2.1.3 {ECO:0000313|EMBL:BAH34741.1};
GN Name=fadD {ECO:0000313|EMBL:BAH34741.1};
GN OrderedLocusNames=RER_40330 {ECO:0000313|EMBL:BAH34741.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH34741.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH34741.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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};
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DR EMBL; AP008957; BAH34741.1; -; Genomic_DNA.
DR RefSeq; WP_020908378.1; NC_012490.1.
DR AlphaFoldDB; C1A2A6; -.
DR KEGG; rer:RER_40330; -.
DR PATRIC; fig|234621.6.peg.4566; -.
DR eggNOG; COG1022; Bacteria.
DR HOGENOM; CLU_000022_45_5_11; -.
DR Proteomes; UP000002204; Chromosome.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
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:SF32; AMP-BINDING DOMAIN-CONTAINING PROTEIN; 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:BAH34741.1}.
FT DOMAIN 24..423
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 597 AA; 63925 MW; C5A7532F336DABEB CRC64;
MSEYSAKAQF TISDNESVVH TVFTHAERTP ELTVFSRPKG EGWVDVTAKE FSEQVTGVAN
GLIAAGVQAG DRVALLSATR YEWTLFDFAI WAAGAATVPI YDSSSQGQVS WILEDSEAVI
AIVETGAHEQ LFQDAPSTLK AVMQIDDGAV EKLTAQGADV DDTELKKRLA GIKADDLASL
VYTSGTTGRP KGCILTHRNF LSEVRGILTA SIGKVAVPGN RVLTFLPLAH VLARAVSLAT
FEAGASQAHW SDFATITTQF ERYKPNTILG VPRVFEKVRD GAARKAESGG KMPGAIFAFA
EATAKEYSQA LDKGGPSLIL KAKHAVADKL VYSKLRAALG GECWFAISGG GALTPELGHF
FRGLGVPIYE GYGLTETTAA HCVNVPGAQK IGTVGQPMGG NGVRIAEDGE IELNGGVVFK
GYWKNDKATE ETFVNGWMRT GDLGELDSDG YLSITGRKKD LLVTAGGKNV SPGPMEDRIR
SHSIVSQAVV VGDGKTYITA LLTVDPEVFE KWKSENGKPS GATVAELRDD KDLRAELQKA
VDDANAAVSH AESIKKFVIL DRDLTEEDGE MTATLKIKRN VVVDRFSKEI EGMYAKS
//