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Database: UniProt
Entry: A0A021VVS1_9CELL
LinkDB: A0A021VVS1_9CELL
Original site: A0A021VVS1_9CELL 
ID   A0A021VVS1_9CELL        Unreviewed;       651 AA.
AC   A0A021VVS1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:EYR65261.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:EYR65261.1};
GN   Name=sdhA {ECO:0000313|EMBL:EYR65261.1};
GN   ORFNames=N866_00350 {ECO:0000313|EMBL:EYR65261.1};
OS   Actinotalea ferrariae CF5-4.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Actinotalea.
OX   NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR65261.1, ECO:0000313|Proteomes:UP000019753};
RN   [1] {ECO:0000313|EMBL:EYR65261.1, ECO:0000313|Proteomes:UP000019753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF5-4 {ECO:0000313|EMBL:EYR65261.1,
RC   ECO:0000313|Proteomes:UP000019753};
RA   Chen F., Li Y., Wang G.;
RT   "Actinotalea ferrariae CF5-4.";
RL   Submitted (JAN-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:EYR65261.1}.
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DR   EMBL; AXCW01000001; EYR65261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A021VVS1; -.
DR   Proteomes; UP000019753; 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:EYR65261.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019753}.
FT   DOMAIN          50..455
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          516..650
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        344
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   651 AA;  71927 MW;  A72ED7676C313CC9 CRC64;
     MTETLVDGLY REGAPILDTT APTGPIEQRW SERTFSARLV NPANRRKLKV IIIGTGLAGA
     SAGATLGEAG YQVTSFCYQD SPRRAHSIAA QGGINASKNY RNDGDSTYRL FYDTIKGGDF
     RSRESNVYRL AELSGNIIDQ CVAQGVPFAR EYGGLLDNRS FGGVQVSRTF YARGQTGQQL
     LLGAYQALER QISAGTVAMY TRHEMLELVV IDGRARGVIV RDMVTGQIET HLADAVVLAT
     GGYSNVFFLS TNAMGCNATA IWRAHRQGAL FANPCYTQIH PTCIPVSGEY QSKLTLMSES
     LRNDGRIWVP AAKADARDPR EIPEDQRDYY LERTYPAFGN LVPRDIASRA AKKVCDEGRG
     VGPTGLGVYL DFADSIQRLG KETVIARYGN LFDMYQRITG EDPYEVPMRI YPAVHYTMGG
     LWVDYDLQSN LPGLFVVGEA NFSDHGANRL GASALMQGLA DGYFVLPNTI NDYLAAGPYK
     AVDDDDPAVA QAVGTVRSRI ATFLVAQGTR SVDSFHKELG QIMWEYCGME RTEEGLRHAI
     GRIRALRASF RADVRVLGEA EELNQSLEKA GRVADFMELA ELMCIDALHR RESCGGHFRA
     ESQTSAGEAL RDDERFAYVA AWQWTGDANP PTLRKEDLHY DYVELKQRSY T
//
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