SPCAD_CUPNN
ID SPCAD_CUPNN Reviewed; 395 AA.
AC F8GVD3;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=bcd {ECO:0000312|EMBL:AEI81492.1};
GN OrderedLocusNames=CNE_BB1p00600 {ECO:0000312|EMBL:AEI81492.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OG Plasmid pBB1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1;
RX PubMed=21742890; DOI=10.1128/jb.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1;
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=0.078 mM for 3SP-CoA {ECO:0000269|PubMed:24317404};
CC Vmax=6.10 umol/min/mg enzyme {ECO:0000269|PubMed:24317404};
CC Note=kcat is 4.4 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; CP002879; AEI81492.1; -; Genomic_DNA.
DR RefSeq; WP_013958551.1; NC_015727.1.
DR AlphaFoldDB; F8GVD3; -.
DR SMR; F8GVD3; -.
DR EnsemblBacteria; AEI81492; AEI81492; CNE_BB1p00600.
DR KEGG; cnc:CNE_BB1p00600; -.
DR HOGENOM; CLU_018204_0_2_4; -.
DR OMA; GDKPAIC; -.
DR Proteomes; UP000006798; Plasmid pBB1.
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; Plasmid.
FT CHAIN 1..395
FT /note="3-sulfinopropanoyl-CoA desulfinase"
FT /id="PRO_0000452008"
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 243..244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 366..370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:K4L7X3"
FT BINDING 387
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 395 AA; 42725 MW; 8403DD99E5BE0833 CRC64;
MYSLTNAQKD LQLKARDLAQ CAFAPTAANT DVTEAYPWAN VDRLLTEGFM GMTIPKEYGG
QGRSYHDTVI VIEEMAKACA TMGRITVEAN MGAIGAIMNY GTEEQKKIAA AAVLSGDKPA
ICISEPNAGS AASEMTTRAD RKGDRYILNG EKYWITGGGV SRLHLIFARV FDDGVDQGIC
AFICVREGNS PENLVVGRRL YAMGVRGIPE THLEFRDLQV HKSMLVVPPG GLKRGFASLM
NAYNAQRVGA GTVALGIAQG AFEEAVTYAK ERQQFGRPIA EFQGLQWMIS DMSIQLEAAR
LLLHAAACSG ESFPDIAMAA RAKIFAAETA NKVTNDSLQI YGSSGYGRHN PMERHVRDAR
MFTIAGGTAQ ILRTQVAGSI LDMKLPQTRG GFLPK
