SPCAD_ADVMD
ID SPCAD_ADVMD Reviewed; 401 AA.
AC K4L7X3;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=3-sulfinopropanoyl-CoA desulfinase {ECO:0000305};
DE EC=3.13.1.4 {ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676};
DE AltName: Full=3-sulfinopropionyl coenzyme A desulfinase {ECO:0000303|PubMed:23354747};
DE Short=3-sulfinopropionyl-CoA desulfinase {ECO:0000305};
DE Short=3SP-CoA desulfinase {ECO:0000305};
GN Name=acd {ECO:0000303|PubMed:23354747};
GN ORFNames=MIM_c31390 {ECO:0000312|EMBL:AHG65203.1};
OS Advenella mimigardefordensis (strain DSM 17166 / LMG 22922 / DPN7).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1247726;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 17166 / LMG 22922 / DPN7;
RX PubMed=23354747; DOI=10.1128/jb.02105-12;
RA Schurmann M., Deters A., Wubbeler J.H., Steinbuchel A.;
RT "A novel 3-sulfinopropionyl coenzyme A (3SP-CoA) desulfinase from Advenella
RT mimigardefordensis strain DPN7T acting as a key enzyme during catabolism of
RT 3,3'-dithiodipropionic acid is a member of the acyl-CoA dehydrogenase
RT superfamily.";
RL J. Bacteriol. 195:1538-1551(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17166 / LMG 22922 / DPN7;
RX PubMed=24739217; DOI=10.1099/mic.0.078279-0;
RA Wubbeler J.H., Hiessl S., Schuldes J., Thurmer A., Daniel R.,
RA Steinbuchel A.;
RT "Unravelling the complete genome sequence of Advenella mimigardefordensis
RT strain DPN7T and novel insights in the catabolism of the xenobiotic
RT polythioester precursor 3,3'-dithiodipropionate.";
RL Microbiology 160:1401-1416(2014).
RN [3] {ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEXES WITH FAD AND
RP SUCCINYL-COA, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND
RP MUTAGENESIS OF ARG-84 AND GLN-246.
RC STRAIN=DSM 17166 / LMG 22922 / DPN7;
RX PubMed=26057676; DOI=10.1107/s1399004715006616;
RA Schurmann M., Meijers R., Schneider T.R., Steinbuchel A., Cianci M.;
RT "3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella
RT mimigardefordensis DPN7(T): crystal structure and function of a desulfinase
RT with an acyl-CoA dehydrogenase fold.";
RL Acta Crystallogr. D 71:1360-1372(2015).
CC -!- FUNCTION: Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to
CC propanoyl-CoA by abstraction of sulfite (PubMed:23354747,
CC PubMed:26057676). Does not show dehydrogenase activity
CC (PubMed:23354747). Involved in the degradation of 3,3'-
CC dithiodipropionate (DTDP), a sulfur-containing precursor substrate for
CC biosynthesis of polythioesters (PTEs) (PubMed:23354747).
CC {ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}.
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:23354747, ECO:0000269|PubMed:26057676};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41625;
CC Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:26057676};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.013 mM for 3SP-CoA {ECO:0000269|PubMed:23354747};
CC Vmax=4.19 umol/min/mg enzyme {ECO:0000269|PubMed:23354747};
CC Note=kcat is 3.13 sec(-1). {ECO:0000269|PubMed:23354747};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23354747,
CC ECO:0000269|PubMed:26057676}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene completely impairs growth on
CC DTDP or 3-sulfinopropanoyl (3SP) as the sole carbon source.
CC {ECO:0000269|PubMed:23354747}.
CC -!- MISCELLANEOUS: Does not catalyze the dehydrogenation of acyl-CoA
CC thioesters (PubMed:23354747). The absence of dehydrogenase activity is
CC most probably caused by the absence of a catalytic glutamate residue in
CC either of the two positions conserved throughout the acyl-CoA
CC dehydrogenase family (PubMed:23354747). {ECO:0000269|PubMed:23354747}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; JX535522; AFV08642.1; -; Genomic_DNA.
DR EMBL; CP003915; AHG65203.1; -; Genomic_DNA.
DR RefSeq; WP_025373864.1; NZ_CP003915.1.
DR PDB; 5AF7; X-ray; 1.89 A; A/B=1-401.
DR PDB; 5AHS; X-ray; 2.30 A; A/B/C/D/E/F=1-401.
DR PDBsum; 5AF7; -.
DR PDBsum; 5AHS; -.
DR AlphaFoldDB; K4L7X3; -.
DR SMR; K4L7X3; -.
DR STRING; 1247726.MIM_c31390; -.
DR EnsemblBacteria; AHG65203; AHG65203; MIM_c31390.
DR KEGG; amim:MIM_c31390; -.
DR PATRIC; fig|1247726.3.peg.3460; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_4; -.
DR OrthoDB; 760677at2; -.
DR BioCyc; MetaCyc:MON-18550; -.
DR BRENDA; 3.13.1.4; 10048.
DR Proteomes; UP000019095; Chromosome.
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 3D-structure; FAD; Flavoprotein; Hydrolase; Reference proteome.
FT CHAIN 1..401
FT /note="3-sulfinopropanoyl-CoA desulfinase"
FT /id="PRO_0000452007"
FT BINDING 121..124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26057676,
FT ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26057676,
FT ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS"
FT BINDING 153..156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26057676,
FT ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS"
FT BINDING 243..244
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26057676"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26057676,
FT ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26057676,
FT ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS"
FT BINDING 343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26057676,
FT ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS"
FT BINDING 366..370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26057676,
FT ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS"
FT BINDING 387
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26057676,
FT ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS"
FT SITE 84
FT /note="Important for activity"
FT /evidence="ECO:0000269|PubMed:26057676"
FT MUTAGEN 84
FT /note="R->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26057676"
FT MUTAGEN 246
FT /note="Q->E: Slight decrease in catalytic efficiency, but
FT still acts as a desulfinase. Does not gain acyl-CoA
FT dehydrogenase activity."
FT /evidence="ECO:0000269|PubMed:26057676"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:5AF7"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 175..185
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 210..221
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 242..271
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 283..308
FT /evidence="ECO:0007829|PDB:5AF7"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 316..340
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:5AF7"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:5AF7"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:5AF7"
SQ SEQUENCE 401 AA; 43531 MW; 3FC28DD46398636B CRC64;
MYELTPEQRT LQTQARELAQ SVFASTAVQT DLTEQYPWDN VAQLRDAGFM GMMLPTSVGG
RGLSTLDTVI VIEEMAKACA TMGRITVDSN LGAIGAITKY GSEEQIKLAA DLVLAGDKPA
ICISEPNAGS AASEMTTRAD KNGDHYILNG EKYWITGGGV SKLHLIFARV FDDGVEQGIG
AFITVLDDHG PEGLKVGRRL YAMGVRGIPE THLEFHDLKI HKSMMITFPD GLKRGFAALM
SAYNAQRVGA GAVALGIAQC AFEEGVAYLK RREQFGRPLA EFQGLQWMVA DMSVQLEAAR
LMLRSAAVSG ETFPDINKAA QAKIFAAETA NKVTNDALQF FGSSGYGRHN PMERHVRDAR
MFTIAGGTAQ ILRTQVASKI LDMKLPQTRD GYLKAAQNSK R
