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Database: UniProt
Entry: A0A0Q0V9Z4_9SPHI
LinkDB: A0A0Q0V9Z4_9SPHI
Original site: A0A0Q0V9Z4_9SPHI 
ID   A0A0Q0V9Z4_9SPHI        Unreviewed;       659 AA.
AC   A0A0Q0V9Z4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KQB99429.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:KQB99429.1};
GN   Name=sdhA {ECO:0000313|EMBL:KQB99429.1};
GN   ORFNames=AQF98_17825 {ECO:0000313|EMBL:KQB99429.1};
OS   Pedobacter sp. Hv1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQB99429.1, ECO:0000313|Proteomes:UP000050543};
RN   [1] {ECO:0000313|EMBL:KQB99429.1, ECO:0000313|Proteomes:UP000050543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hv1 {ECO:0000313|EMBL:KQB99429.1,
RC   ECO:0000313|Proteomes:UP000050543};
RA   Ott B.M., Beka L., Graf J., Rio R.;
RT   "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT   Medicinal Leech Mucosal Castings.";
RL   Submitted (OCT-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:KQB99429.1}.
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DR   EMBL; LLWP01000009; KQB99429.1; -; Genomic_DNA.
DR   RefSeq; WP_055133321.1; NZ_LLWP01000009.1.
DR   AlphaFoldDB; A0A0Q0V9Z4; -.
DR   STRING; 1740090.AQF98_17825; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000050543; Unassembled WGS sequence.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
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   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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KQB99429.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050543}.
FT   DOMAIN          37..463
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          525..658
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        331
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   659 AA;  72900 MW;  CB97A302974AAC97 CRC64;
     MSALNSNIPE GELTNKWTKF KSSVPLVNPS NKRSLEVIVV GSGLAGASAA ATLAEMGYKV
     KCFCFQDSPR RAHSIAAQGG INAAKNYQND GDSTYRLFYD TIKGGDYRAR EANVHRLAEV
     SANIIDQCVA QGVPLAREYG GLLDNRSFGG TQVQRTFYAA GQTGQQLLLG AYSALERQIG
     MGKVEMFTRH EMLEVVKIDG KARGIIARNL ITGELERHFG HAVVLGTGGY GNVFFLSTNA
     MGSNVTAAWK ANKQGAFFAN PCYTQIHPTC IPVSGDHQSK LTLMSESLRN DGRIWVPKKK
     DDTRKASDIP EDERDYYLER RYPAFGNLVP RDVASRAAKE RCDAGYGVGS SKLAVYLDFK
     ANTERYGKIE ASKAGNHNPD QETCFRLGTE VIKEKYGNLF DMYAQITGEN PYEMPMRIYP
     AVHYTMGGLW VDYNLMTTVP GLYCTGEANF SDHGANRLGA SALMQGLADG YFVLPYTIGA
     YLSKEISVKA IPTDHPAFVE AEAKAKGILD TLIGIKGTKS VDYFHKKLGL IMWEKCGMAR
     NAEGLKSAIA EIQQLKKDFW SDVRVPGDSN EYNPELEKAG RVADFIELGE LMCLDALNRN
     ESCGGHFREE YQTEEGEALR DDENYAYVAA WENKGDGTFE LHKEELKFEN IKIAQRSYK
//
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