ID A0A4U8UJA3_9HELI Unreviewed; 657 AA.
AC A0A4U8UJA3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=LS72_003380 {ECO:0000313|EMBL:TLE16313.1};
OS Helicobacter apodemus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=135569 {ECO:0000313|EMBL:TLE16313.1, ECO:0000313|Proteomes:UP000029920};
RN [1] {ECO:0000313|EMBL:TLE16313.1, ECO:0000313|Proteomes:UP000029920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT-03-7007 {ECO:0000313|EMBL:TLE16313.1,
RC ECO:0000313|Proteomes:UP000029920};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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:TLE16313.1}.
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DR EMBL; JRPC02000007; TLE16313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U8UJA3; -.
DR Proteomes; UP000029920; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR Gene3D; 3.10.20.820; -; 1.
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; 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; IPR014006; Succ_Dhase_FrdA_Gneg.
DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR PANTHER; PTHR11632:SF71; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 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.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029920};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..410
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 468..597
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 657 AA; 73060 MW; 226590617F4F3AE6 CRC64;
MKIIYCDSLV IGGGLAGLRA AVACQSKGLN TIVLSLIPVK RSHSAAAQGG MQASLGNSKM
SDGDNEDLHF ADTVKGSDWG CDQKVARMFV TTAPKAIRQL AAWGVPWTRI KKGDRTAIIN
AQKTTITEED FRHGLIHSRD FGGTKKWRTC YTADATGHTM LFAVANEALK HDVTIHDRKE
AIALIHKDKR CYGAIVRDLI TGELIGYVAK GTLIATGGYG RIYKDTTNAV ICEGIGSAIA
LETGVAKLGN MEAVQFHPTA LFPSGILLTE GCRGDGGVLR DVDGYRFMPD YEPEKKELAS
RDVVARRMIQ RIREGKGVQS PYGEHLWLDI SILGRQHIET NLRDVQEICE CFAGIDPAEK
WAPVKPMQHY SMGGIRTNYK GETALEGLFS AGEAACWDLH GFNRLGGNSV SEAVVSGMII
GDYFAQSCQN TYATIETKLV EEFIQKQQTY LNNILTSEGK ENVFEIKNRM KEIMGEKVGI
FRDGTHLKEA VDELEQLYIR SQNIAIKTKR LEANPELEEA YRVPKMLKIA LCVAKGALDR
TESRGAHSRE DYPKRDDVNW LKRTLASWED PNQTLPTLTY ESLDIATMEI APGFRGYGAK
GMIIENPESL RRQEEIDKIR SDMEAQGKDR YAIQEALMPF DLQAYYKTRN ERIGDKQ
//
