IPDF_MYCTU
ID IPDF_MYCTU Reviewed; 262 AA.
AC I6YCF0;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=(5R,7aS)-5-hydroxy-7a-methyl-1-oxo-2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-CoA reductase {ECO:0000305};
DE EC=1.1.1.- {ECO:0000305|PubMed:28377529};
GN Name=ipdF {ECO:0000303|PubMed:28377529};
GN OrderedLocusNames=Rv3559c {ECO:0000312|EMBL:CCP46381.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=Erdman;
RX PubMed=28377529; DOI=10.1128/mbio.00321-17;
RA Crowe A.M., Casabon I., Brown K.L., Liu J., Lian J., Rogalski J.C.,
RA Hurst T.E., Snieckus V., Foster L.J., Eltis L.D.;
RT "Catabolism of the last two steroid rings in Mycobacterium tuberculosis and
RT other bacteria.";
RL MBio 8:e00321-e00321(2017).
CC -!- FUNCTION: Involved in the final steps of cholesterol and steroid
CC degradation (PubMed:28377529). Probably catalyzes the oxidation of the
CC 5-OH group of (5R,7aS)-5-hydroxy-7a-methyl-1-oxo-2,3,5,6,7,7a-
CC hexahydro-1H-indene-carboxyl-CoA, leading to the formation of HIEC-CoA
CC (Probable). {ECO:0000269|PubMed:28377529, ECO:0000305|PubMed:28377529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5R,7aS)-5-hydroxy-7a-methyl-1-oxo-2,3,5,6,7,7a-hexahydro-1H-
CC indene-carboxyl-CoA + NAD(+) = (7aS)-7a-methyl-1,5-dioxo-
CC 2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:66356, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:167096, ChEBI:CHEBI:167100;
CC Evidence={ECO:0000305|PubMed:28377529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66357;
CC Evidence={ECO:0000305|PubMed:28377529};
CC -!- ACTIVITY REGULATION: Requires the presence of IpdC.
CC {ECO:0000305|PubMed:28377529}.
CC -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC {ECO:0000269|PubMed:28377529}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46381.1; -; Genomic_DNA.
DR RefSeq; NP_218076.1; NC_000962.3.
DR RefSeq; WP_003900097.1; NZ_NVQJ01000014.1.
DR AlphaFoldDB; I6YCF0; -.
DR SMR; I6YCF0; -.
DR STRING; 83332.Rv3559c; -.
DR PaxDb; I6YCF0; -.
DR PRIDE; I6YCF0; -.
DR DNASU; 887897; -.
DR GeneID; 887897; -.
DR KEGG; mtu:Rv3559c; -.
DR PATRIC; fig|83332.111.peg.3964; -.
DR TubercuList; Rv3559c; -.
DR eggNOG; COG1028; Bacteria.
DR OMA; WEVANVI; -.
DR PhylomeDB; I6YCF0; -.
DR BioCyc; MetaCyc:G185E-7836-MON; -.
DR UniPathway; UPA01058; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006707; P:cholesterol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome; Steroid metabolism; Sterol metabolism.
FT CHAIN 1..262
FT /note="(5R,7aS)-5-hydroxy-7a-methyl-1-oxo-2,3,5,6,7,7a-
FT hexahydro-1H-indene-carboxyl-CoA reductase"
FT /id="PRO_0000452309"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 77..78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
SQ SEQUENCE 262 AA; 27430 MW; B7EB2D76BB321B36 CRC64;
MNLSVAPKEI AGHGLLDGKV VVVTAAAGTG IGSATARRAL AEGADVVISD HHERRLGETA
AELSALGLGR VEHVVCDVTS TAQVDALIDS TTARMGRLDV LVNNAGLGGQ TPVADMTDDE
WDRVLDVSLT SVFRATRAAL RYFRDAPHGG VIVNNASVLG WRAQHSQSHY AAAKAGVMAL
TRCSAIEAAE YGVRINAVSP SIARHKFLDK TASAELLDRL AAGEAFGRAA EPWEVAATIA
FLASDYSSYL TGEVISVSCQ HP
