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Database: UniProt
Entry: A0A263DUP5_9PSEU
LinkDB: A0A263DUP5_9PSEU
Original site: A0A263DUP5_9PSEU 
ID   A0A263DUP5_9PSEU        Unreviewed;       645 AA.
AC   A0A263DUP5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:OZM81095.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:OZM81095.1};
GN   Name=sdhA {ECO:0000313|EMBL:OZM81095.1};
GN   ORFNames=CFP66_17035 {ECO:0000313|EMBL:OZM81095.1};
OS   Pseudonocardia sp. MH-G8.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1854588 {ECO:0000313|EMBL:OZM81095.1, ECO:0000313|Proteomes:UP000216936};
RN   [1] {ECO:0000313|EMBL:OZM81095.1, ECO:0000313|Proteomes:UP000216936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MH-G8 {ECO:0000313|EMBL:OZM81095.1,
RC   ECO:0000313|Proteomes:UP000216936};
RA   Wang J., Leiva S., Huang J., Huang Y.;
RT   "Non-contiguous finished genome sequence and description of Pseudonocardia
RT   marinum sp. nov., an obligate marine actinomycete from a macroalgal
RT   phycosphere.";
RL   Submitted (JUL-2017) 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:OZM81095.1}.
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DR   EMBL; NKYF01000006; OZM81095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A263DUP5; -.
DR   OrthoDB; 9805351at2; -.
DR   Proteomes; UP000216936; 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:OZM81095.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216936}.
FT   DOMAIN          47..452
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          512..644
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   645 AA;  70497 MW;  33CC2E24882C014A CRC64;
     MSTYADFTIG DPVVDTAAPD GPIETRWERR RFGVKLVNPA NKRKMKVIVV GTGLAGGSAA
     ATLAELGYQV SSFCYQDSPR RAHSIAAQGG INAAKNYRGD GDSIHRLFYD TVKGGDFRSR
     ESNVHRLAEI SVQIIDQCVA QGVPFAREYG GLLDTRSFGG AQVSRTFYAR GQTGQQLLLG
     AYQALERQID AGGVTMYPRH EMLELIVVDG RARGIVARDL VTGETRTHLA DAVVLASGGY
     GNVFYLSTNA KGCNVTASWR AHRKGALFAN PCYTQIHPTC IPVSGDHQSK LTLMSESLRN
     DGRVWVPQKA GDTRAPGDIP EAERDYFLER QYPAFGNLVP RDIASRAAKN VCDAGRGVGP
     TGLGVYLDFA DAIGRLGRSA VAAKYGNLFQ MYQRITGEDP YAVPMRIFPA VHYTMGGLWV
     DYDLQSSIPG LFVVGEANFS DHGANRLGAS ALMQGLADGY FVLPNTIGDY LARGVEPVAA
     DAPEVREAEQ AVADRVTTLL TIDGDRTVDS FHRELGHIMW DHCGMERTEE GLRKALDRIP
     ELRREFWQSV KVPGSAATLN QSLEKAGRVA DFLELGELMC LDALHREESC GGHFRAESQT
     DDGEAARDDE RFSYAAAWEY TGAAPVLHKE DLTFDYVTPS QRSYK
//
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