CASI_RHOJR
ID CASI_RHOJR Reviewed; 555 AA.
AC Q0S4D7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Steroid-22-oyl-CoA synthetase {ECO:0000303|PubMed:24244004};
DE EC=6.2.1.- {ECO:0000269|PubMed:21987574, ECO:0000269|PubMed:23024343, ECO:0000269|PubMed:24244004};
DE AltName: Full=Steroid-CoA synthetase {ECO:0000303|PubMed:23024343};
GN Name=casI {ECO:0000303|PubMed:21987574};
GN OrderedLocusNames=RHA1_ro05822 {ECO:0000312|EMBL:ABG97599.1};
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 CATALYTIC ACTIVITY.
RX PubMed=21987574; DOI=10.1074/jbc.m111.289975;
RA Capyk J.K., Casabon I., Gruninger R., Strynadka N.C., Eltis L.D.;
RT "Activity of 3-ketosteroid 9alpha-hydroxylase (KshAB) indicates cholesterol
RT side chain and ring degradation occur simultaneously in Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 286:40717-40724(2011).
RN [3]
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 [4]
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 ATP-dependent formation of CoA
CC thioesters of steroids with isopropanoyl side chains, likely occurring
CC as degradation intermediates (PubMed:23024343, PubMed:24244004). Can
CC use 4-BNC, HSBNC and HIDP as substrate (PubMed:23024343,
CC PubMed:24244004). {ECO:0000269|PubMed:23024343,
CC ECO:0000269|PubMed:24244004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxochol-4-en-22-oate + ATP + CoA = 3-oxochol-4-en-22-oyl-CoA
CC + AMP + diphosphate; Xref=Rhea:RHEA:43872, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:83777,
CC ChEBI:CHEBI:83792, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:21987574, ECO:0000269|PubMed:23024343,
CC ECO:0000269|PubMed:24244004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43873;
CC Evidence={ECO:0000269|PubMed:21987574, ECO:0000269|PubMed:23024343,
CC ECO:0000269|PubMed:24244004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-9-oxo-9,10-seco-chola-1,3,5-trien-22-oate + ATP +
CC CoA = 3-hydroxy-9-oxo-9,10-seco-chola-1,3,5-trien-22-oyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:43876, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:83794,
CC ChEBI:CHEBI:83797, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:24244004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43877;
CC Evidence={ECO:0000269|PubMed:24244004};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for 4-BNC {ECO:0000269|PubMed:24244004};
CC KM=500 uM for HSBNC {ECO:0000269|PubMed:24244004};
CC KM=190 uM for HIDP {ECO:0000269|PubMed:24244004};
CC Note=kcat is 18 sec(-1) with 4-BNC as substrate. kcat is 1.4 sec(-1)
CC with HSBNC as substrate. kcat is 60 sec(-1) with HIDP 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; ABG97599.1; -; Genomic_DNA.
DR RefSeq; WP_011597926.1; NC_008268.1.
DR AlphaFoldDB; Q0S4D7; -.
DR SMR; Q0S4D7; -.
DR STRING; 101510.RHA1_ro05822; -.
DR SwissLipids; SLP:000001001; -.
DR EnsemblBacteria; ABG97599; ABG97599; RHA1_ro05822.
DR KEGG; rha:RHA1_ro05822; -.
DR PATRIC; fig|101510.16.peg.5861; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_10_11; -.
DR OMA; GATFFTY; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IEA:InterPro.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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 InterPro; IPR030310; FadD17/FadD6-like.
DR PANTHER; PTHR43107:SF15; PTHR43107:SF15; 1.
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..555
FT /note="Steroid-22-oyl-CoA synthetase"
FT /id="PRO_0000452102"
SQ SEQUENCE 555 AA; 61164 MW; D581C7F7669102F4 CRC64;
MELERTTIAR MLFDRLGDDR LGVRTREQDW TWDEVVRESA ARGAVASSLR RDGPFHVGVL
LENTPEFLFW LGGAALAGAA VVGVNPTRRG AELEAEIRYV DCQLIVTDTA GKAQLAGLDL
GLSEDRFLLV DDPAYTELVA AHAVESPAED PGIDASTLFL LLFTSGTTGT SKAVRCSQGR
LARLAYANTA KYGHVREDVD YCCMPLFHGN ALMALWAPAL ANGATVCLPR KFSASGFLPD
VRFFGATFFT YVGKALAYLM ATPEQPDDRD NTLVRGFGTE ASPEDKTEFV RRFGAELYEG
YGSSEGAGSV TLDPDAPEGA LGRPANENIV IVDPDTRVEK ARARLDEHGR VLNPDEAIGE
MVDKAGASRF EGYYKNEDAI ADRIRHGWYW TGDLGYVDEA GFIYFAGRKG DWIRVDGENT
SALMVERILR RHPKVVATGV FAVPDPRSGD QVMAAVEVAD PTDFDPAEFA AFLGNQDDLG
TKAAPRFVRV SRDLPVTGSN KVLKRTLQEQ RWRCDDPVFR WVGRGVPEYH EMTDSEKAVL
EQEFHTHGRQ RFLHV
