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Entry: G0A6S5_METMM
LinkDB: G0A6S5_METMM
Original site: G0A6S5_METMM 
ID   G0A6S5_METMM            Unreviewed;       594 AA.
AC   G0A6S5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|ARBA:ARBA00019965, ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU362051};
GN   OrderedLocusNames=Metme_2141 {ECO:0000313|EMBL:AEG00546.1};
OS   Methylomonas methanica (strain MC09).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG00546.1, ECO:0000313|Proteomes:UP000008888};
RN   [1] {ECO:0000313|EMBL:AEG00546.1, ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|EMBL:AEG00546.1,
RC   ECO:0000313|Proteomes:UP000008888};
RX   PubMed=22123758; DOI=10.1128/JB.06267-11;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA   Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA   Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L., Murrell J.C.;
RT   "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT   methanica MC09.";
RL   J. Bacteriol. 193:7001-7002(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MC09;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA   Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA   Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L.Y., Murrell C.;
RT   "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT   methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT   "Complete sequence of Methylomonas methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000030,
CC         ECO:0000256|RuleBase:RU362051};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362051};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (bacterial route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004894, ECO:0000256|RuleBase:RU362051}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004515, ECO:0000256|RuleBase:RU362051};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004515,
CC       ECO:0000256|RuleBase:RU362051}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004515, ECO:0000256|RuleBase:RU362051}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040,
CC       ECO:0000256|RuleBase:RU362051}.
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DR   EMBL; CP002738; AEG00546.1; -; Genomic_DNA.
DR   RefSeq; WP_013818790.1; NC_015572.1.
DR   AlphaFoldDB; G0A6S5; -.
DR   STRING; 857087.Metme_2141; -.
DR   KEGG; mmt:Metme_2141; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_6_1_6; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000008888; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; 4.10.80.40; succinate dehydrogenase protein 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; IPR003952; FRD_SDH_FAD_BS.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   NCBIfam; TIGR01816; sdhA_forward; 1.
DR   NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 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.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|RuleBase:RU362051};
KW   Cell membrane {ECO:0000256|RuleBase:RU362051};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU362051};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR611281-4};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362051};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362051};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008888};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          13..407
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          462..594
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   MOD_RES         49
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   594 AA;  64989 MW;  8CF537F546E0382A CRC64;
     MASAYNIIEH QHDVVVVGAG GAGLRATFGM VEKGLKTACI TKVFPTRSHT VAAQGGISAA
     LGNMGEDDWR FHMYDTVKGS DWLGDQDAIE YMCREAIPAI IELEHYGVPF SRTPEGKIYQ
     RAFGGMSTHY GKGQAQRTCA AADVTGHAIL HTLYQQALKH KAEFFVEYIA LDLIMEDGEC
     RGVLAWCLDD GSIHLFRGHQ TVLATGGYGR TFLSCTSAHT VTGDGNGMAL RAGLPLQDME
     FVQFHPTGIY GSGCLMSEGA RGEGGYLTNS EGEAFMVRYA PHVKDLASRD VVSRAITVEL
     NEGRGVGPKK DHVYLHLEHL DPAIIHERLP GITETARIFA GVDATKQPIP VLPTVHYNMG
     GIPTNYKAEV VTLKDGNPDY VVPGLMAIGE TACVSVHGAN RLGSNSLLDL VVFGRAAAIR
     CTELIKPGMP HKPLATDATD KALTRFDKIR HANGSRTTAE IRLDMQTTMQ SKAAVFRTEK
     TLQEGIQRMG EVAASFEDVK VGDKSLIWNT DLVETLELDN LLGQAQVTIT AAGNRQESRG
     GHAREDFPKR DDENWMKHTL TWRENNQVKI DCRPVHLYTL TDEVDVVAPK ERVY
//
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