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Database: UniProt
Entry: A0A0Q7BBM1_9ACTN
LinkDB: A0A0Q7BBM1_9ACTN
Original site: A0A0Q7BBM1_9ACTN 
ID   A0A0Q7BBM1_9ACTN        Unreviewed;       677 AA.
AC   A0A0Q7BBM1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KQW49932.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:KQW49932.1};
GN   Name=sdhA {ECO:0000313|EMBL:KQW49932.1};
GN   ORFNames=ASC77_25655 {ECO:0000313|EMBL:KQW49932.1};
OS   Nocardioides sp. Root1257.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW49932.1, ECO:0000313|Proteomes:UP000051939};
RN   [1] {ECO:0000313|EMBL:KQW49932.1, ECO:0000313|Proteomes:UP000051939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1257 {ECO:0000313|EMBL:KQW49932.1,
RC   ECO:0000313|Proteomes:UP000051939};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW49932.1, ECO:0000313|Proteomes:UP000051939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1257 {ECO:0000313|EMBL:KQW49932.1,
RC   ECO:0000313|Proteomes:UP000051939};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQW49932.1}.
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DR   EMBL; LMDV01000005; KQW49932.1; -; Genomic_DNA.
DR   RefSeq; WP_056150832.1; NZ_LMDV01000005.1.
DR   AlphaFoldDB; A0A0Q7BBM1; -.
DR   STRING; 1736439.ASC77_25655; -.
DR   OrthoDB; 9805351at2; -.
DR   Proteomes; UP000051939; 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   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:KQW49932.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT   DOMAIN          65..476
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          537..676
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        361
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   677 AA;  74736 MW;  6D84E6825B1B1567 CRC64;
     MPDTTLTSDP SHDEPGDHGD DAAGYYTPGE PIKDTKAPTG PIDERWQTRK FEARLVNPSN
     RRKLDVIIVG TGLAGGAAAA TLGEAGYNVK SFCYQDSPRR AHSIAAQGGI NAAKNYKEDG
     DSVHRLFYDT VKGGDYRSRE SNVYRLAEVS TNIIDQCVAQ GVPFAREYGG LLDNRSFGGV
     QVSRTFYARG QTGQQLLIGA YQAMERQVAA GTVEQFTRHE MLEVIVVDGK ARGIIARDLV
     TGEIETHLAD VVVLASGGYG NVFFLSTNAM GSNVTAAWRA HRKGAYMANP CYTQIHPTCI
     PVTGTHQSKL TLMSESLRND GRIWVPKSKA DCDKDPRDIP EEARDYYLER IYPSFGNLVP
     RDIASRAAKN VCDEGRGVGP EVDGVRRGVY LDFSAAIARL GKDGIEEKYD NLFDMYARIT
     GENPYETPMR IYPAVHYVMG GLWVDYDLQS SIEGLFVTGE ANFSDHGANR LGASALMQGL
     ADGYFVLPHT IRDYLADGPF EKVAEDHPAV VEAKKAVEDR VAHFLNTSGT RSVDSYHREL
     GNIMWEYCGM ERSEDGLKKA IDLIRTLKDD FWRNVKVLGT AEGLNQSLER AGRVADFFEL
     GELMCIDALN RRESCGGHFR AESQTEDGEA LRHDDQFAYV AAWEFAGDPD SGGMGTPVLH
     KEELVYTAIE MKQRSYK
//
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