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P0AC43 (SDHA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate dehydrogenase flavoprotein subunit

EC=1.3.5.1
Gene names
Name:sdhA
Ordered Locus Names:Z0877, ECs0748
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (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 + a quinone = fumarate + a quinol.

Cofactor

FAD.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1.

Subunit structure

Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic anchor protein. The complex forms trimers By similarity.

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Succinate dehydrogenase flavoprotein subunit
PRO_0000158653

Regions

Nucleotide binding14 – 196FAD By similarity
Nucleotide binding37 – 5216FAD By similarity
Nucleotide binding404 – 4052FAD By similarity

Sites

Active site2861Proton acceptor By similarity
Binding site2211FAD By similarity
Binding site2421Substrate By similarity
Binding site2541Substrate By similarity
Binding site3541Substrate By similarity
Binding site3881FAD By similarity
Binding site3991Substrate By similarity

Amino acid modifications

Modified residue451Tele-8alpha-FAD histidine By similarity
Modified residue2671N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AC43 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 837F9A63991B6CE8

FASTA58864,422
        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 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
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. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG55047.1.
BA000007 Genomic DNA. Translation: BAB34171.1.
PIRD90722.
RefSeqNP_286439.1. NC_002655.2.
NP_308775.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0AC43.
SMRP0AC43. Positions 1-588.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z0877.

Proteomic databases

PRIDEP0AC43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG55047; AAG55047; Z0877.
BAB34171; BAB34171; BAB34171.
GeneID917480.
957829.
KEGGece:Z0877.
ecs:ECs0748.
PATRIC18350518. VBIEscCol44059_0770.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000160475.
KOK00239.
OMARTEQGRI.
OrthoDBEOG6M3PC4.

Enzyme and pathway databases

BioCycECOL386585:GJFA-743-MONOMER.
ECOO157:SDHA-MONOMER.
UniPathwayUPA00223; UER01005.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSDHA_ECO57
AccessionPrimary (citable) accession number: P0AC43
Secondary accession number(s): P10444, P78282
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways