NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).

Comments

FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth (By similarity).
CATALYTIC ACTIVITY: Succinate + acceptor = fumarate + reduced acceptor.
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle .
SUBUNIT: Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and an hydrophobic anchor protein. The complex forms trimers (By similarity).
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).
SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE005174; AAG55047.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB34171.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D90722; D90722.

RefSeq

NP_286439.1; -.
NP_308775.1; -.

3D structure databases

SMR

P0AC43; 1-588.

ModBase

P0AC43.

Enzyme and pathway databases

BioCyc

ECOL83334:ECS0748-MON; -.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000104;	Molecular function: succinate dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR003953; FAD_bind2_N.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR003952; FRD_SDH_FAD_BS.
IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
IPR011281; Succ_DHase_flav_su_fwd.
IPR014006; Succ_Dhase_frdA_Gneg.
Graphical view of domain structure.

Pfam

PF00890; FAD_binding_2; 1.
PF02910; Succ_DH_flav_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.

TIGRFAMs

TIGR01816; sdhA_forward; 1.
TIGR01812; sdhA_frdA_Gneg; 1.

PROSITE

PS00504; FRD_SDH_FAD_BINDING; 1.

BLOCKS

P0AC43.

Genome annotation databases

GeneID

917480; -.
957829; -.

GenomeReviews

BA000007_GR; ECs0748.
AE005174_GR; Z0877.

KEGG

ece:Z0877; -.
ecs:ECs0748; -.

Phylogenomic databases

HOGENOM

P0AC43; -.

Genome annotation databases

CMR

P0AC43; Z0877.

Other

ProtoNet

P0AC43.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Electron transport; FAD; Flavoprotein; Membrane; Oxidoreductase; Transport; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 588`	`588`	`Succinate dehydrogenase flavoprotein subunit.`	`PRO_0000158653`
`NP_BIND`	`37 52`	`16`	`FAD (By similarity).`
`ACT_SITE`	`286 286`		`Proton acceptor (By similarity).`
`BINDING`	`242 242`		`Substrate (By similarity).`
`BINDING`	`254 254`		`Substrate (By similarity).`
`BINDING`	`354 354`		`Substrate (By similarity).`
`BINDING`	`399 399`		`Substrate (By similarity).`
`MOD_RES`	`45 45`		`Tele-8alpha-FAD histidine (By similarity).`

Sequence information

Length: 588 AA [This is the length of the unprocessed precursor]

Molecular weight: 64422 Da [This is the MW of the unprocessed precursor]

CRC64: 837F9A63991B6CE8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ GGITVALGNT 

        70         80         90        100        110        120 
HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE HMGLPFSRLD DGRIYQRPFG 

       130        140        150        160        170        180 
GQSKNFGGEQ AARTAAAADR TGHALLHTLY QQNLKNHTTI FSEWYALDLV KNQDGAVVGC 

       190        200        210        220        230        240 
TALCIETGEV VYFKARATVL ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ 

       250        260        270        280        290        300 
FHPTGIAGAG VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG 

       310        320        330        340        350        360 
RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI PTCHYMMGGI 

       370        380        390        400        410        420 
PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL GGNSLLDLVV FGRAAGLHLQ 

       430        440        450        460        470        480 
ESIAEQGALR DASESDVEAS LDRLNRWNNN RNGEDPVAIR KALQECMQHN FSVFREGDAM 

       490        500        510        520        530        540 
AKGLEQLKVI RERLKNARLD DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH 

       550        560        570        580 
SRFDFPDRDD ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY

P0AC43 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools