ID FADD3_COMTE Reviewed; 540 AA.
AC Q7WSH3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-MAY-2023, entry version 44.
DE RecName: Full=3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoyl:CoA ligase {ECO:0000303|PubMed:16891113};
DE Short=HIP:CoA ligase {ECO:0000303|PubMed:16891113};
DE EC=6.2.1.41 {ECO:0000250|UniProtKB:P96843};
GN Name=fadD3 {ECO:0000250|UniProtKB:P96843};
GN Synonyms=ORF18 {ECO:0000303|PubMed:16891113};
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TA441;
RX PubMed=12902225; DOI=10.1128/aem.69.8.4421-4430.2003;
RA Horinouchi M., Hayashi T., Yamamoto T., Kudo T.;
RT "A new bacterial steroid degradation gene cluster in Comamonas testosteroni
RT TA441 which consists of aromatic-compound degradation genes for seco-
RT steroids and 3-ketosteroid dehydrogenase genes.";
RL Appl. Environ. Microbiol. 69:4421-4430(2003).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=TA441;
RX PubMed=16891113; DOI=10.1016/j.jsbmb.2006.06.006;
RA Horinouchi M., Hayashi T., Koshino H., Kudo T.;
RT "ORF18-disrupted mutant of Comamonas testosteroni TA441 accumulates
RT significant amounts of 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid
RT and its derivatives after incubation with steroids.";
RL J. Steroid Biochem. Mol. Biol. 101:78-84(2006).
CC -!- FUNCTION: Involved in the catabolism of the rings C and D of
CC cholesterol. Catalyzes the ATP-dependent CoA thioesterification of
CC 3aalpha-H-4alpha(3'-propanoate)-7abeta-methylhexahydro-1,5-indanedione
CC (HIP) to yield HIP-CoA. {ECO:0000269|PubMed:16891113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-
CC yl]propanoate + ATP + CoA = 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-
CC octahydro-1H-inden-4-yl]propanoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:41640, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:63692, ChEBI:CHEBI:78357,
CC ChEBI:CHEBI:456215; EC=6.2.1.41;
CC Evidence={ECO:0000250|UniProtKB:P96843};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate 9,17-dioxo-
CC 1,2,3,4,10,19-hexanorandrostan-5-oic acid (HIP) when incubated with
CC 1,4-androstadiene-3,17-dione (ADD). {ECO:0000269|PubMed:16891113}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB076368; BAC81695.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7WSH3; -.
DR SMR; Q7WSH3; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR CDD; cd17638; FadD3; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cholesterol metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Steroid metabolism; Sterol metabolism.
FT CHAIN 1..540
FT /note="3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-
FT inden-4-yl]propanoyl:CoA ligase"
FT /id="PRO_0000430640"
FT BINDING 189..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 540 AA; 58510 MW; 9E5BC9F9FA421460 CRC64;
MSKPNQNAMP ESSLTLPGML ADVVSRFAGR AAIVENGKSI SYAQLQQLSR LAARALMSLG
VQAGDRVALW APNLSEWIVA ACGVHAAGGV LVPLNTRMKG AEAADILERS RARVLVCVGD
FLNNYYPDLL NGLRPVTLQQ VVVLGDKVLP SADMNWAQFM ARADGTTAEA QQQREARIKP
DDTADLMFTS GTTGRPKGVM CAHRPTILAF KAWSDVVGLT EGSRYLIVNP FFHTFGYKAG
WVAALLQGST VYPEQIFDAQ AILHRIESDR ISFLPGPPTL FLSMLAHPGL KNFDLSSLKS
SVTGASTVPP ILIKRMREEL GIMNVTTAYG LTECGGCATL CEPSDNVETV ANTCGKALPG
TEVRCVDEQG RPVGPGEAGE VLLRGYHIMQ GYFEDEKATE ETIDADGWLH TGDVGVLDER
GYLRITDRLK DMFIVGGFNC YPAEIERMLS NHPEVAQVAV VGVADERMGE VGCACVVTRN
GVTLDQEAFI AWCRANMANY KVPRFVLQLD GLPVNASNKV QKRDLLQIVK DRLASVPQPA
//
