SPCAD_PARXL
ID SPCAD_PARXL Reviewed; 388 AA.
AC Q13PC1;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 ORFNames=Bxe_B1901 {ECO:0000312|EMBL:ABE34068.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=LB400;
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=0.027 mM for 3SP-CoA {ECO:0000269|PubMed:24317404};
CC Vmax=1.58 umol/min/mg enzyme {ECO:0000269|PubMed:24317404};
CC Note=kcat is 1.1 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; CP000271; ABE34068.1; -; Genomic_DNA.
DR RefSeq; WP_011491418.1; NZ_CP008762.1.
DR AlphaFoldDB; Q13PC1; -.
DR SMR; Q13PC1; -.
DR STRING; 266265.Bxe_B1901; -.
DR EnsemblBacteria; ABE34068; ABE34068; Bxe_B1901.
DR KEGG; bxb:DR64_7210; -.
DR KEGG; bxe:Bxe_B1901; -.
DR PATRIC; fig|266265.5.peg.5834; -.
DR eggNOG; COG1960; Bacteria.
DR OMA; GDKPAIC; -.
DR OrthoDB; 760677at2; -.
DR Proteomes; UP000001817; Chromosome 2.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
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.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Hydrolase; Reference proteome.
FT CHAIN 1..388
FT /note="3-sulfinopropanoyl-CoA desulfinase"
FT /id="PRO_0000452009"
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 240..241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 336
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 363..367
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 384
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 388 AA; 41875 MW; 9BCF1700246A3E21 CRC64;
MFELTDAQRQ LQQSARRLAL EAIAPHAAQT DRSEQYPWHT VEALREQRLM GMTLPPEYGG
KGASYFDTVL VIEELSKVCA ASGRIMVESN MGAIGAIMKY GSDAQKQLAA RLVLAGDKPA
ICITEPQAGS AASDMQTRAE RRGDTWHLSG CKHWITGGGV SKLHFVFARA IEDGKDTGIA
GFIVVGPDVP GMTIQRIPAM GIRGVPEARI EFDDMRVRHD MKVTPPGRTE AGFAGLMNAY
NAQRVGAATV ALGIAQGAFD LALDYAKRRE QFGRPIAEFQ GLQWMLADMS IQLEAARLMV
WKAAASGSEF PSMFAAAQAK IAAGEAAIKV TNDALQIHGA VGYGRDLPLE RMVRDARMFT
ISGGTAQILR TQVAGTLLGQ KLSQRRSA
