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Database: UniProt
Entry: A0A132PNS6_9MYCO
LinkDB: A0A132PNS6_9MYCO
Original site: A0A132PNS6_9MYCO 
ID   A0A132PNS6_9MYCO        Unreviewed;       636 AA.
AC   A0A132PNS6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KWX23953.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:KWX23953.1};
GN   Name=sdhA {ECO:0000313|EMBL:KWX23953.1};
GN   ORFNames=AFM11_11285 {ECO:0000313|EMBL:KWX23953.1};
OS   Mycolicibacterium wolinskyi.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX23953.1, ECO:0000313|Proteomes:UP000070612};
RN   [1] {ECO:0000313|EMBL:KWX23953.1, ECO:0000313|Proteomes:UP000070612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC_01 {ECO:0000313|EMBL:KWX23953.1,
RC   ECO:0000313|Proteomes:UP000070612};
RA   de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA   Limbago B.M., Noble-Wang J.;
RT   "A draft genome sequence of Mycobacterium wolinskyi.";
RL   Submitted (JUL-2015) 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:KWX23953.1}.
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DR   EMBL; LGTW01000006; KWX23953.1; -; Genomic_DNA.
DR   RefSeq; WP_067848149.1; NZ_LGTW01000006.1.
DR   AlphaFoldDB; A0A132PNS6; -.
DR   STRING; 59750.AWC31_30610; -.
DR   PATRIC; fig|59750.3.peg.6334; -.
DR   Proteomes; UP000070612; 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   GO; GO:0008152; P:metabolic process; 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; 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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KWX23953.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070612}.
FT   DOMAIN          10..429
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          485..590
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   COILED          498..525
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   636 AA;  70295 MW;  5A6A8763C4922577 CRC64;
     MVELERHSYD VVVIGAGGAG LRAVIEARER GLRVAVVTKS LFGKAHTVMA EGGCAAAMRN
     VNTKDSWQVH FGDTMRGGKF LNNWRMAELH AQEAPDRVWE LETYGALFDR TKDGRISQRN
     FGGHTYPRLA HVGDRTGLEI IRTLQQKIVS LQQEDKRELG DYDARIRVFH ECSITELIKD
     GDRIAGAFGY WRETGNFVLF EAPAVVLATG GIGKSFKVSS NSWEYTGDGH ALALRAGSSL
     INMEFIQFHP TGMVWPLSVK GILVTEGVRG DGGVLKNSEG KRFMFDYIPS VFKGQYAETE
     EEADQWLKDN DSARRTPDLL PRDEVARAIN SEVKAGRGSP HGGVYLDIAS RMPPEEIKRR
     LPSMYHQFIE LAEVDITKDE MEVGPTCHYV MGGIEVDPDT GAGATPGLFA AGECSGGMHG
     SNRLGGNSLS DLLVFGRRAG LGASEYVRAL ADRPKVTEAA VEDATRMALA PFDKHDNPEN
     PYTLHAELQQ SMNDLVGIIR KEEEIEAALT KLAELKARYA NVTVEGGRVF NPGWHLAIDM
     RNMLLVSECV AKAALQRTES RGGHTRDDYP EMDAKWRNTL LVCRTVDNDD SVVPDVSVTP
     EPQVPMRPDL LGCFELSELE KYYTDAELAE HPERKG
//
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