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Database: UniProt
Entry: A0A095Z218_9ACTO
LinkDB: A0A095Z218_9ACTO
Original site: A0A095Z218_9ACTO 
ID   A0A095Z218_9ACTO        Unreviewed;       658 AA.
AC   A0A095Z218;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KGF02539.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:KGF02539.1};
GN   Name=sdhA {ECO:0000313|EMBL:KGF02539.1};
GN   ORFNames=HMPREF1628_01215 {ECO:0000313|EMBL:KGF02539.1};
OS   Actinomyces sp. S4-C9.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=1219581 {ECO:0000313|EMBL:KGF02539.1, ECO:0000313|Proteomes:UP000035029};
RN   [1] {ECO:0000313|EMBL:KGF02539.1, ECO:0000313|Proteomes:UP000035029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4-C9 {ECO:0000313|EMBL:KGF02539.1,
RC   ECO:0000313|Proteomes:UP000035029};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGF02539.1}.
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DR   EMBL; JRMU01000002; KGF02539.1; -; Genomic_DNA.
DR   RefSeq; WP_034506866.1; NZ_JRMU01000002.1.
DR   AlphaFoldDB; A0A095Z218; -.
DR   eggNOG; COG1053; Bacteria.
DR   Proteomes; UP000035029; Unassembled WGS sequence.
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   PRINTS; PR00368; FADPNR.
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:KGF02539.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035029}.
FT   DOMAIN          51..461
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          523..657
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   658 AA;  73304 MW;  473FB8137C691D63 CRC64;
     MTDQLIHGLY REGEKIADTK APLDVPLAQC WETRKFNAKL VNPANRRKLK VIIVGTGLAG
     GAAAASLGEM GYHVDAFFYQ DSARRAHSIA AQGGINAAKN YRNDNDSVFR LFYDTVKGGD
     YRARETNVYR LAEVSANIID QCVAQGVPFA REYGGLLDNR SFGGVQVSRT FYARGQTGQQ
     LLIGAYQALE RQVEAGTVVE HRRHEMVELI VSDGRARGIV ARNMATGELE TYTADAVVLA
     TGGYGNVFFL STNAMGCNGT AVWRAHRKGA YFGNPCYTQI HPTCIPQHGD QQSKLTLMSE
     SLRNDGRIWV PKKAEDCKKD PRDIPEEDRD YYLERIYPSF GNLVPRDIAS RQAKNMCDDG
     RGVGPEINGV ARGVYLDFAE AIERMGKDAV SAKYGNLFDM YERITGDNPY EVPMRIYPAV
     HYTMGGLWVD YDLQSNLPGL FVAGEANFSD HGANRLGASA LMQGLSDGYF VLPNTINDYL
     AGAFGFDKLD ENSPAVQEAL DSTQARIDKL MSIDGNRSVD SFHKELGHIM WEYCGMERNE
     EGLKKAIGMI RELREEFYNN VRIPGKTKGE MNQSLEKAGR VADFLELGEL MCIDALHREE
     SCGGHFRAEH QTPEGEALRH DDKFTYVAAW EFGADGVPTL HKEDLIYNNI ELKQRSYK
//
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