CASG_RHOJR
ID CASG_RHOJR Reviewed; 553 AA.
AC Q0S4D9;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Steroid-24-oyl-CoA synthetase {ECO:0000303|PubMed:24244004};
DE EC=6.2.1.- {ECO:0000269|PubMed:23024343, ECO:0000269|PubMed:24244004};
DE AltName: Full=Cholyl-CoA synthetase {ECO:0000303|PubMed:23024343};
DE AltName: Full=Steroid-CoA synthetase {ECO:0000303|PubMed:23024343};
GN Name=casG {ECO:0000303|PubMed:23024343};
GN OrderedLocusNames=RHA1_ro05820 {ECO:0000312|EMBL:ABG97597.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION.
RC STRAIN=RHA1;
RX PubMed=23024343; DOI=10.1128/jb.01169-12;
RA Mohn W.W., Wilbrink M.H., Casabon I., Stewart G.R., Liu J.,
RA van der Geize R., Eltis L.D.;
RT "Gene cluster encoding cholate catabolism in Rhodococcus spp.";
RL J. Bacteriol. 194:6712-6719(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=RHA1;
RX PubMed=24244004; DOI=10.1128/jb.01012-13;
RA Casabon I., Swain K., Crowe A.M., Eltis L.D., Mohn W.W.;
RT "Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain
RT catabolism.";
RL J. Bacteriol. 196:579-587(2014).
CC -!- FUNCTION: Involved in cholate catabolism (PubMed:23024343,
CC PubMed:24244004). Catalyzes the transformation of cholate to cholyl-
CC CoA, thus initiating degradation of the C5 cholate side chain
CC (PubMed:23024343, PubMed:24244004). Can also catalyze the ATP-dependent
CC formation of CoA thioesters of deoxycholate and chenodeoxycholate
CC (PubMed:23024343). {ECO:0000269|PubMed:23024343,
CC ECO:0000269|PubMed:24244004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholate + CoA = AMP + choloyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:23532, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23024343,
CC ECO:0000269|PubMed:24244004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23533;
CC Evidence={ECO:0000269|PubMed:23024343, ECO:0000269|PubMed:24244004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + deoxycholate = AMP + deoxycholoyl-CoA +
CC diphosphate; Xref=Rhea:RHEA:47128, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58810, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23024343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47129;
CC Evidence={ECO:0000269|PubMed:23024343};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + chenodeoxycholate + CoA = AMP + chenodeoxycholoyl-CoA +
CC diphosphate; Xref=Rhea:RHEA:43764, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62989, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23024343, ECO:0000269|PubMed:24244004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43765;
CC Evidence={ECO:0000269|PubMed:23024343, ECO:0000269|PubMed:24244004};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=160 uM for cholate {ECO:0000269|PubMed:24244004};
CC Note=kcat is 2.4 sec(-1) with cholate as substrate.
CC {ECO:0000269|PubMed:24244004};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:23024343,
CC ECO:0000269|PubMed:24244004}.
CC -!- INDUCTION: Up-regulated on cholate. {ECO:0000269|PubMed:23024343}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CP000431; ABG97597.1; -; Genomic_DNA.
DR RefSeq; WP_011597924.1; NC_008268.1.
DR AlphaFoldDB; Q0S4D9; -.
DR SMR; Q0S4D9; -.
DR STRING; 101510.RHA1_ro05820; -.
DR SwissLipids; SLP:000000990; -.
DR EnsemblBacteria; ABG97597; ABG97597; RHA1_ro05820.
DR KEGG; rha:RHA1_ro05820; -.
DR PATRIC; fig|101510.16.peg.5859; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_11; -.
DR OMA; GWWVPRE; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Lipid metabolism; Nucleotide-binding;
KW Reference proteome; Steroid metabolism.
FT CHAIN 1..553
FT /note="Steroid-24-oyl-CoA synthetase"
FT /id="PRO_0000452101"
SQ SEQUENCE 553 AA; 60484 MW; 3B9E58A37E7E9656 CRC64;
MTAPTDPQLH LDQVMSRLTG PGGRFELVEE PVLGTRMPVM KNRGRSVGEL LTTSLRWGDR
DYLVTADRRM SYTEHAAAVA ALATALREDY GVRKGDRVAI LAANTPEWVV AFWATQVLGA
ISVGLNGWWV PREVEYGLTH SRPTVVVADA KRAETLAAVG TDLPVLTMEE DLPALFARYA
GSPMPHTDVD EDDPAAILYT SGTSGRPKGA LHSQRNILAV VDYHRFSDAV VGEFSGRPVD
PAVPSPLRYL LTSPLFHIAS LHNLVIPRLA TGGAVVMHQG GFDVDAVLRL VERERVTNWG
AVPTMASRLV EHDDLDKYDL SSLTSFSLAS APSSVAFKER LREKVPFARN ALVDSYGLTE
CSTAIAVATA PELEQFPGTL GRPIITVSME IRDPYGEWLP DGVEGEVCVR SPFVMLGYWE
DEAATAAAIA PGRWLRTGDY GLVENGRLRL TGRRSDLILR GGENVYPTEI EQCLDEHPEV
LECAVIGTPH EDLGQEVAAV VVLRPGAAAT EAELREYAAD RLSYFKVPTR WRITTDLLPR
NATGKMVRRD ITV
