ID A0A0M3RJ68_9ACTO Unreviewed; 667 AA.
AC A0A0M3RJ68;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:ALC98586.1};
DE EC=1.3.5.1 {ECO:0000313|EMBL:ALC98586.1};
GN Name=sdhA {ECO:0000313|EMBL:ALC98586.1};
GN ORFNames=AM609_02220 {ECO:0000313|EMBL:ALC98586.1};
OS Actinomyces sp. oral taxon 414.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=712122 {ECO:0000313|EMBL:ALC98586.1, ECO:0000313|Proteomes:UP000061022};
RN [1] {ECO:0000313|Proteomes:UP000061022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0588 {ECO:0000313|Proteomes:UP000061022};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012590; ALC98586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3RJ68; -.
DR STRING; 712122.AM609_02220; -.
DR KEGG; acq:AM609_02220; -.
DR PATRIC; fig|712122.3.peg.500; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000061022; Chromosome.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ALC98586.1}.
FT DOMAIN 50..470
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 533..666
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 667 AA; 74890 MW; DE668B97ABBBC918 CRC64;
MMTHLIDGLY RQGEPIADTK APHDVPIARR WEQRKFNAQL VNPANRRKLD IIVVGSGLAG
GAAAASLGEQ GYNVKCFFYQ DSARRAHSIA AQGGINAAKN YRNDGDSVYR LFYDTVKGGD
YRAREDNVYR LAEVSANIID QCVAQGVPFA REYGGLLDNR SFGGVQVSRT FYARGQTGQQ
LLIGAYQALE RQVHAGTVKE FRRHEMVELI VVDGRARGIV ARDMVSGQIE THLADAVVLA
TGGYGNVFFL STNAMGCNGT AIWRAYRKGA YFANPCYTQI HPTCIPQSGD FQSKLTLMSE
SLRNDGRIWV PKRAEDCDKD PRTIPEEDRD YYLERIYPAF GNLVPRDIAS RQAKNMCDEG
RGVGPAIREK APDGTERMMR RGVYLDFSEA IGRLGRDAVS ARYGNLFEMY QRITGDDPYE
VPMRIYPAVH YTMGGLWVDY DLESNIPGLY IGGEANFSDH GANRLGASAL MQGLADGYFV
LPDTMNDYLA DMLRLGKVDP DAPEIAQAKR SVEERIARLM ALEGSRSVDD FHMALGRIMW
EYCGMERRDA GLREAIGQIR ELKEEFWRDA RVTGEAMELN QSLEKAGRLL DFFELAELMC
IDALHRRESC GGHFRAESQT PEGEAMRHDD EFLYVAAWEW GGEDAPPILH KEALIYKDIE
LKQRSYK
//
