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P0AC49

- FRDB_ECO57

UniProt

P0AC49 - FRDB_ECO57

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Protein

Fumarate reductase iron-sulfur subunit

Gene

frdB

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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 activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi58 – 581Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi63 – 631Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi66 – 661Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi149 – 1491Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi152 – 1521Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi155 – 1551Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi159 – 1591Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi205 – 2051Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi211 – 2111Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi215 – 2151Iron-sulfur 2 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 3 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  4. electron carrier activity Source: InterPro
  5. metal ion binding Source: UniProtKB-KW
  6. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciECOL386585:GJFA-5141-MONOMER.
ECOO157:FRDB-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate reductase iron-sulfur subunit (EC:1.3.5.1)
Gene namesi
Name:frdB
Ordered Locus Names:Z5760, ECs5134
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 244243Fumarate reductase iron-sulfur subunitPRO_0000158699Add
BLAST

Interactioni

Subunit structurei

Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins.By similarity

Protein-protein interaction databases

STRINGi155864.Z5760.

Structurei

3D structure databases

ProteinModelPortaliP0AC49.
SMRiP0AC49. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 97822Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini140 – 169304Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
KOiK00245.
OMAiCHFAASC.
OrthoDBiEOG6CK7MG.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AC49-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP
60 70 80 90 100
DLSYRWSCRM AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE
110 120 130 140 150
RDLVVDMTHF IESLEAIKPY IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI
160 170 180 190 200
NCGLCYAACP QFGLNPEFIG PAAITLAHRY NEDSRDHGKK ERMAQLNSQN
210 220 230 240
GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT LKPR
Length:244
Mass (Da):27,123
Last modified:January 23, 2007 - v2
Checksum:iAC1D7A73244D7AC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG59354.1.
BA000007 Genomic DNA. Translation: BAB38557.1.
PIRiF86111.
F91270.
RefSeqiNP_290788.1. NC_002655.2.
NP_313161.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG59354; AAG59354; Z5760.
BAB38557; BAB38557; BAB38557.
GeneIDi914097.
959968.
KEGGiece:Z5760.
ecs:ECs5134.
PATRICi18359889. VBIEscCol44059_5080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG59354.1 .
BA000007 Genomic DNA. Translation: BAB38557.1 .
PIRi F86111.
F91270.
RefSeqi NP_290788.1. NC_002655.2.
NP_313161.1. NC_002695.1.

3D structure databases

ProteinModelPortali P0AC49.
SMRi P0AC49. Positions 2-244.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z5760.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG59354 ; AAG59354 ; Z5760 .
BAB38557 ; BAB38557 ; BAB38557 .
GeneIDi 914097.
959968.
KEGGi ece:Z5760.
ecs:ECs5134.
PATRICi 18359889. VBIEscCol44059_5080.

Phylogenomic databases

eggNOGi COG0479.
HOGENOMi HOG000160590.
KOi K00245.
OMAi CHFAASC.
OrthoDBi EOG6CK7MG.

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-5141-MONOMER.
ECOO157:FRDB-MONOMER.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view ]
Pfami PF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view ]
SUPFAMi SSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR00384. dhsB. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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.
    , 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.

Entry informationi

Entry nameiFRDB_ECO57
AccessioniPrimary (citable) accession number: P0AC49
Secondary accession number(s): P00364
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3