SPCAD_VARPD
ID SPCAD_VARPD Reviewed; 399 AA.
AC B9U6P5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=3-sulfinopropanoyl-CoA desulfinase {ECO:0000305};
DE EC=3.13.1.4 {ECO:0000269|PubMed:24317404};
DE AltName: Full=3-sulfinopropionyl coenzyme A desulfinase {ECO:0000303|PubMed:24317404};
DE Short=3-sulfinopropionyl-CoA desulfinase {ECO:0000305};
DE Short=3SP-CoA desulfinase {ECO:0000303|PubMed:24317404};
GN Name=acd {ECO:0000303|PubMed:24317404};
GN Synonyms=acdA {ECO:0000312|EMBL:KLN58429.1};
GN ORFNames=VPARA_05440 {ECO:0000312|EMBL:KLN58429.1};
OS Variovorax paradoxus.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=34073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=19001372; DOI=10.1074/jbc.m806762200;
RA Bruland N., Wubbeler J.H., Steinbuchel A.;
RT "3-mercaptopropionate dioxygenase, a cysteine dioxygenase homologue,
RT catalyzes the initial step of 3-mercaptopropionate catabolism in the 3,3-
RT thiodipropionic acid-degrading bacterium variovorax paradoxus.";
RL J. Biol. Chem. 284:660-672(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBEA6;
RA Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA Daniel R.;
RT "Genome sequence of Variovorax paradoxus TBEA6.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=TBEA6;
RX PubMed=24317404; DOI=10.1128/jb.01265-13;
RA Schuermann M., Demming R.M., Krewing M., Rose J., Wuebbeler J.H.,
RA Steinbuechel A.;
RT "Identification of 3-sulfinopropionyl coenzyme A (CoA) desulfinases within
RT the Acyl-CoA dehydrogenase superfamily.";
RL J. Bacteriol. 196:882-893(2014).
CC -!- FUNCTION: Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to
CC propanoyl-CoA by abstraction of sulfite. Does not show dehydrogenase
CC activity. {ECO:0000269|PubMed:24317404}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfinopropanoyl-CoA + H2O = H(+) + propanoyl-CoA + sulfite;
CC Xref=Rhea:RHEA:41624, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:57392, ChEBI:CHEBI:78349; EC=3.13.1.4;
CC Evidence={ECO:0000269|PubMed:24317404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41625;
CC Evidence={ECO:0000269|PubMed:24317404};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:24317404};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:K4L7X3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.052 mM for 3SP-CoA {ECO:0000269|PubMed:24317404};
CC Vmax=3.47 umol/min/mg enzyme {ECO:0000269|PubMed:24317404};
CC Note=kcat is 2.5 sec(-1). {ECO:0000269|PubMed:24317404};
CC -!- SUBUNIT: Homotrimer or homotetramer. {ECO:0000269|PubMed:24317404}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; EU449952; ACC69031.2; -; Genomic_DNA.
DR EMBL; JZWI01000003; KLN58429.1; -; Genomic_DNA.
DR RefSeq; WP_047783180.1; NZ_JZWI01000003.1.
DR AlphaFoldDB; B9U6P5; -.
DR SMR; B9U6P5; -.
DR EnsemblBacteria; KLN58429; KLN58429; VPARA_05440.
DR PATRIC; fig|34073.19.peg.546; -.
DR Proteomes; UP000035170; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Hydrolase; Reference proteome.
FT CHAIN 1..399
FT /note="3-sulfinopropanoyl-CoA desulfinase"
FT /id="PRO_0000452010"
FT BINDING 121..124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 153..156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 244..245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 273
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 367..371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT SITE 84
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
SQ SEQUENCE 399 AA; 42951 MW; C5D6273936A45DD2 CRC64;
MYDLTSAQLD LQARARELAQ TKFAPTAAQT DQTEEYPWKN VELLRDAGFM GMTLPKSIGG
QGLSYLDAVI VVEEMAKACA TMGRITVEAN MGAIGAIAKY GTPEQLKIAA DLVLAGDKPA
ICISEPNAGS AASEMTTRAD RQGDHYIING EKYWITGGGV SKVHLIFARV LEDGVDQGIG
GFICVRDGEN SPAGLVIGRR LYAMGVRGIP ETHIEFHDLK VHKSMLVVPP GGLKRGFASL
MTAYNAQRVG AGTVALGIAQ GAFEEGLERL KTRHQFGRPI AEFQGLQWMA ADMSTQLEAA
RLLLRHAAAS GEEFPDIDKA ARAKIFAAET ANKVTNDALQ FWGSSGYGRE NPMERHVRDA
RMFTIAGGTA QILRTQVAGK LLGMKLPQTR DGFAKVAAR
