IPDC_MYCTU
ID IPDC_MYCTU Reviewed; 355 AA.
AC P71847; F2GER3; I6X7M5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-1H-indene-4-carboxyl-CoA dehydrogenase {ECO:0000305};
DE Short=5OH-HIC-CoA dehydrogenase {ECO:0000305};
DE EC=1.3.1.- {ECO:0000305|PubMed:28377529};
GN Name=ipdC {ECO:0000303|PubMed:28377529};
GN OrderedLocusNames=Rv3553 {ECO:0000312|EMBL:CCP46375.1};
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
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 introduction of a
CC double bound into the C ring of 5OH-HIC-CoA, leading to the formation
CC of (5R,7aS)-5-hydroxy-7a-methyl-1-oxo-3,5,6,7-tetrahydro-2H-indene-4-
CC carboxyl-CoA (Probable). {ECO:0000269|PubMed:28377529,
CC ECO:0000305|PubMed:28377529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-1H-indene-
CC 4-carboxyl-CoA + NAD(+) = (5R,7aS)-5-hydroxy-7a-methyl-1-oxo-
CC 2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:66352, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:167058, ChEBI:CHEBI:167096;
CC Evidence={ECO:0000305|PubMed:28377529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66353;
CC Evidence={ECO:0000305|PubMed:28377529};
CC -!- ACTIVITY REGULATION: Requires the presence of IpdF.
CC {ECO:0000305|PubMed:28377529}.
CC -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC {ECO:0000269|PubMed:28377529}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant does not grow on cholesterol, but
CC grows as the wild-type on glycerol. In the presence of cholesterol,
CC disruption mutant accumulates 5OH-HIC-CoA.
CC {ECO:0000269|PubMed:28377529}.
CC -!- SIMILARITY: Belongs to the nitronate monooxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP46375.1; -; Genomic_DNA.
DR RefSeq; NP_218070.1; NC_000962.3.
DR RefSeq; WP_003419324.1; NZ_NVQJ01000014.1.
DR AlphaFoldDB; P71847; -.
DR SMR; P71847; -.
DR STRING; 83332.Rv3553; -.
DR PaxDb; P71847; -.
DR DNASU; 887190; -.
DR GeneID; 45427537; -.
DR GeneID; 887190; -.
DR KEGG; mtu:Rv3553; -.
DR PATRIC; fig|83332.111.peg.3958; -.
DR TubercuList; Rv3553; -.
DR eggNOG; COG2070; Bacteria.
DR InParanoid; P71847; -.
DR OMA; IDDLPSC; -.
DR PhylomeDB; P71847; -.
DR BioCyc; MetaCyc:G185E-7830-MON; -.
DR UniPathway; UPA01058; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006707; P:cholesterol catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04730; NPD_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004136; NMO.
DR Pfam; PF03060; NMO; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Flavoprotein; FMN; Lipid metabolism; NAD;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Steroid metabolism;
KW Sterol metabolism.
FT CHAIN 1..355
FT /note="(3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-
FT 1H-indene-4-carboxyl-CoA dehydrogenase"
FT /id="PRO_0000452307"
FT BINDING 21..23
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9I4V0"
FT BINDING 173..175
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9I4V0"
FT BINDING 196..197
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9I4V0"
SQ SEQUENCE 355 AA; 36831 MW; 2C3660DCC505E768 CRC64;
MRLRTPLTEL IGIEHPVVQT GMGWVAGARL VSATANAGGL GILASATMTL DELAAAITKV
KAVTDKPFGV NIRADAADAG DRVELMIREG VRVASFALAP KQQLIARLKE AGAVVIPSIG
AAKHARKVAA WGADAMIVQG GEGGGHTGPV ATTLLLPSVL DAVAGTGIPV IAAGGFFDGR
GLAAALCYGA AGVAMGTRFL LTSDSTVPDA VKRRYLQAGL DGTVVTTRVD GMPHRVLRTE
LVEKLESGSR ARGFAAALRN AGKFRRMSQM TWRSMIRDGL TMRHGKELTW SQVLMAANTP
MLLKAGLVDG NTEAGVLASG QVAGILDDLP SCKELIESIV LDAITHLQTA SALVE
