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Database: UniProt
Entry: M7NXX8_9GAMM
LinkDB: M7NXX8_9GAMM
Original site: M7NXX8_9GAMM 
ID   M7NXX8_9GAMM            Unreviewed;       649 AA.
AC   M7NXX8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:EMR12061.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:EMR12061.1};
GN   Name=sdhA {ECO:0000313|EMBL:EMR12061.1};
GN   ORFNames=MPL1_12371 {ECO:0000313|EMBL:EMR12061.1};
OS   Methylophaga lonarensis MPL.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR12061.1, ECO:0000313|Proteomes:UP000012019};
RN   [1] {ECO:0000313|EMBL:EMR12061.1, ECO:0000313|Proteomes:UP000012019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MPL {ECO:0000313|EMBL:EMR12061.1,
RC   ECO:0000313|Proteomes:UP000012019};
RX   PubMed=23661481;
RA   Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA   Murrell J.C., Shouche Y.S.;
RT   "Draft Genome Sequence of Methylophaga lonarensis MPLT, a Haloalkaliphilic
RT   (Non-Methane-Utilizing) Methylotroph.";
RL   Genome Announc. 1:E00202-13(2013).
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:EMR12061.1}.
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DR   EMBL; APHR01000075; EMR12061.1; -; Genomic_DNA.
DR   RefSeq; WP_009727417.1; NZ_APHR01000075.1.
DR   AlphaFoldDB; M7NXX8; -.
DR   STRING; 1286106.MPL1_12371; -.
DR   PATRIC; fig|1286106.3.peg.2472; -.
DR   eggNOG; COG1053; Bacteria.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000012019; 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   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:EMR12061.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012019}.
FT   DOMAIN          42..452
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          514..648
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        337
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   649 AA;  71944 MW;  29B3ECAC2234B79C CRC64;
     MMESLPFDFD AHCPKGPLDQ RWTQHKYHLQ VVSPANRKHY KVIVVGTGLA GASAAASLAE
     MGYQVESFCF QDSPRRAHSI AAQGGINAAK NYHNDGDSVW RLFYDMIKGG DFRARESNVF
     RLAELSTSII DQAVAQGVPF AREYSGYLAN RSFGGAQVSR TFYARGQTGQ QLLLGAYQAM
     SRQIAAGRIT QHSRCEMQDL IMLNGQAKGI VSRNLVTGEL QAHLADCVVL CTGGYGNAFY
     LSTNAKGCNT SAIWRAHKHG ALFANPCFTQ IHPTCIPQHG ELQSKLTLMS ESLRNDGRIW
     APKDIADCDK APATIAEQQR DYFLERLYPA FGNLVPRDIA SRAVKHICDA GRGVGVEIAG
     QRRGVYLDFA DAIAQQGLDV INEKYGNLFD MYERITAEDP RQTPMRIYPA VHYTMGGLWV
     DYNLMTTVDG LFAGGEANFS DHGANRLGAS ALMQGLADGY FILPATVSDY LAKQHPIRPQ
     DFAAEARNAI ETVRLRLDRL MNAPSPETAP DVFHRELGEI LWHACGMARE ASQLKSAITE
     IQQLRERFWQ HVKVTGSSDT LNQTLERAAR VADFLELGEL MCLDALQREE SCGCHARVEH
     LTDGGEVQRD DMQFASVSAW QYSGDVSEPR LLQEPLLFEF VSPGVRSYR
//
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