ID C7MVC7_SACVD Unreviewed; 638 AA.
AC C7MVC7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Succinate dehydrogenase subunit A {ECO:0000313|EMBL:ACU97756.1};
GN OrderedLocusNames=Svir_27750 {ECO:0000313|EMBL:ACU97756.1};
OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS 12207 / P101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU97756.1, ECO:0000313|Proteomes:UP000000841};
RN [1] {ECO:0000313|EMBL:ACU97756.1, ECO:0000313|Proteomes:UP000000841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC {ECO:0000313|Proteomes:UP000000841};
RX PubMed=21304650; DOI=10.4056/sigs.20263;
RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Saccharomonospora viridis type strain
RT (P101).";
RL Stand. Genomic Sci. 1:141-149(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR630664-51};
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DR EMBL; CP001683; ACU97756.1; -; Genomic_DNA.
DR RefSeq; WP_015787068.1; NC_013159.1.
DR AlphaFoldDB; C7MVC7; -.
DR STRING; 471857.Svir_27750; -.
DR KEGG; svi:Svir_27750; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_8_1_11; -.
DR Proteomes; UP000000841; Chromosome.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW FAD {ECO:0000256|PIRSR:PIRSR630664-51};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR630664-
KW 51}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000841}.
FT DOMAIN 10..429
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 489..603
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 501..528
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 322
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT BINDING 15..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 38..53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 428..429
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
SQ SEQUENCE 638 AA; 70608 MW; 2002D46A2B7F4B7D CRC64;
MTEVERHSYD VVVIGAGGAG LRAVIEARQR GLSVAVVSKS LFGKAHTVMA EGGCAASMGN
VNPNDGWQVH FRDTMRGGKF LNDWRMAELH AKEAPDRVWE LETYGALFDR TPDGRISQRN
FGGHTYPRLA HVGDRTGLEL IRTMQQKIVS LQQEDYAAHG DYEAKLKVFD ECTITELLTQ
DGAIAGAFGY WRESGRFVLF EAPAVILATG GIGKSFQVTS NSWEYTGDGH ALALRAGATL
INMEFVQFHP TGMVWPPSVK GILVTEGVRG DGGVLRNSEG ERFMFRYIPD VFKGQYAETE
EEADRWYEDP DNNRRTPDLL PRDEVARAIN TEVKEGRGSP HGGVFLDIAS RLPAEEIKRR
LPSMYHQFKE LADVDITAEP MEVGPTCHYV MGGIEVDPDT AASSVPGLFA AGECAGGMHG
SNRLGGNSLS DLLVFGRRAG IGAADYVDSL TSRPTVSAVD LAMAARTALA PFDPPRDGQA
AENPYSLQTE LQQCMNDLVG IIRTASEMEQ ALEKLDEIRE RLRAVTVEGH RQYNPGWHLA
LDLRNMLLVS ECVARSALRR TESRGGHTRD DYPQMDANWR KVLLVCSATD REAPLPRIEV
TTKEQKPMRD DLFALFELSE LEKYYTDEEL AEHPERTA
//
