ID A0A151XDD1_9HYME Unreviewed; 2182 AA.
AC A0A151XDD1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000256|RuleBase:RU362051};
DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN ORFNames=ALC60_02803 {ECO:0000313|EMBL:KYQ58382.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ58382.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ58382.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ58382.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ58382.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH)
CC that is involved in complex II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). {ECO:0000256|RuleBase:RU362051}.
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|RuleBase:RU362051};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR630664-51, ECO:0000256|RuleBase:RU362051};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000256|RuleBase:RU362051}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU362051}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU362051}; Matrix side
CC {ECO:0000256|RuleBase:RU362051}.
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; KQ982294; KYQ58382.1; -; Genomic_DNA.
DR STRING; 64791.A0A151XDD1; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner 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 Pfam; PF13913; zf-C2HC_2; 2.
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 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, ECO:0000256|PIRSR:PIRSR630664-
KW 51};
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:UP000075809};
KW Transit peptide {ECO:0000256|RuleBase:RU362051};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051};
KW Ubiquinone {ECO:0000313|EMBL:KYQ58382.1}.
FT DOMAIN 1581..1975
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 2030..2182
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 89..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1858
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-1"
FT BINDING 1586..1591
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 1609..1624
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 1793
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 1814
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 1826
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 1925
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 1958
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 1969
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 1974..1975
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT MOD_RES 1617
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ SEQUENCE 2182 AA; 246490 MW; D2A5013A34D72F55 CRC64;
MLCCVPKRLA DGGPFYDETL FHDGILFHDE TGNNPPSSIR EIQIELFPKD ALSPILFPCA
ICARTFTLQS LEKHARICER AAAKKRKPFD SAKQRIQGTE LAEFQPKQEI RRHQQDERSR
STWKKTHDDF LRTIREARGD VMDSRKQCNS LISSGAPTRA NEKGTCPTCN RQFGIKAYDR
HVAWCKDRVT RMPMSPATNL AKERLEARMR YRAPTLKNRR AINREKYSPG SAANQAAKAS
LSSPALVKPK ETISSISCNR ESPVKQKPAI MRRPGQLKDS PPSSGPIKSR LVDRMNRPPE
DHDCLLTSTS CRSLHPAISS RRSLYLPVPP TRPKTNDLVS SNKIASPITS SRKQFNQNEM
IFQRIQNDDT RNREICSARM QNIVSARSQG HPRINDIAVN NKTLGITVQP CRIHMNMQKD
DQLVTWKQIS RKKDNFQADD PVINHNFSRE FQLLDLDRLC NREEGNENRN KTEGDLSIIE
DNFIRIDKDS KVDKVKNNDN ITWLSGIQNL NQTYLIKNSE DIEPSEIFHS KWKPIKHSPR
VEFYLKDKED EIKIRKTKIE QVKELKMCIK DKENDNIPVE CKVEKLKTNN KSIKNIQKIN
SEKIEVVAHT TEELNINTIE KNRRVASYEE TKITENDIEK IEINTSIKEG TKEIEKINIA
DITELDKLNV YKEDKKGRQI TMNEIIIENT KYTKEIEQNL SESDQLIKSS LFNVTHSTAS
NVSKKKNFID QSQDCLNSKD EVPHCESDTR YNNSLELKES IATFICDQPN INEITSLNNS
NNQADCNSSP ENETLACQSR NSLDLIENIK KISFPASSPI VTPKKNCTRN VEEIKIDEER
YENGLTNICN KKPKRNSKKL KCEVYSLPQN SEIADGNYLN ASMNKISLHV KNNRQFQEKN
FSSDNIGNIE NNTKNGKTDF NTDSDNSCSN NKSSLLDRSI IKAEITTAEG LRKKNVDSEF
DYGSDNTVLV EEYNRRSTDG LGSSVTLTDY AEEQSQCRGS EIFLNAGMNF PKCAYGAAKR
AAREQSVNSI EMKHRIKESM NLLRGSTDSL ISSVEFVELA SIRRPKANCA YEQEIIEIIR
PNKRYKVFKD LPDIKGDAAE MKEDSEGSYW ERTSKISQNR LTNLYPTCHM EYKLTKRNPR
VRILPPVLNP FSINQRKVEL ETRPAWCNYV RRRPDFNLVL KARTGTCKDY DPFLLAEQQM
NDLLSDTSDQ SITGSPKVQQ TRDTLYPLSH SSAFVKYPPT DKRSSLIMPP TEFDDLLSNF
SSDSTETNSI SREVFLKPNL AGKDATDSAA SKPVRELGRR VIIDKSKALG VDERRGVVSA
DRSRKIFDKD TLRNTGSLIN RSNSIRASSA PRINSGLERK ASGGIRKGSR NVESQKSSDQ
SLNQRNNNYS SLSGSNLSLN SIISSSELDV KRSNSMFDEL MTSFEEDAFP GLRSFLNNES
FDLSSPGGDR QRNGSLISDE ELSSPDSYKP QDHSKLSNDS AYNSLNRKYS HHGRSANDVI
DRLDEDVPRN GTSPTQTMTK CKMSKFCHEC GQRFPETAKF CCECGVKRLA FFHVNVSPAE
KAKCGVEKGG SNYPLIDHCY DVVIVGAGGA GLRAAFGLGK KGYRVAVVSK LFPTRSHTVA
AQGGINAAIA DQQKDNWLYH MYDTVKGSDW LGDQDAIHLL AREAPRAVYE LENYGCPFSR
TEDGRIYQRA FGGQSLKFGK GGQAKRTCAV ADRTGHAVLH TLYGQSLRYD VHYFVEYFAL
DLLMHGRCCK GILAWELETG LLHRFRAHHT VIATGGAERC YFSCTAAHAC TGDGMAIACR
AGLPLQDMEF IQFHPTGIYG SGILITEGSR GEGGKLINSM GEFFMEKYAP VAKDLASRDV
VSRAMTMEIL NGRGVGEKKD HIYLQLTHLP AELIRERLPG ISHLAWVFAG VDVTKQPIPV
IPTVHYNMGG IPTNWRAQVL TRENEEDISI EGLWAAGETA CASVHGANRL GANSLLEIVV
FGKAIADQID CIARPGERHG DLSSDIGEQS ICRFDATRYA KGCVPVAELR EEMQRTMQKY
CGVFRTCDIL QRGCREMSRL YTCDLPDLCV QDQSLIWNTE LVEALELQNM MLVCMHTVYA
AENRKESRGS HAREDFKDRI DEYDYTKPLE GQKKRPYTEH WRKHSLTWAQ EDGTIYISYR
PVIDTTLDET EAQHVPPAVR AY
//
