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P20921

- FRDB_PROVU

UniProt

P20921 - FRDB_PROVU

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Protein
Fumarate reductase iron-sulfur subunit
Gene
frdB
Organism
Proteus vulgaris
Status
Reviewed - Annotation score: 4 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.

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Binds 1 2Fe-2S cluster.
Binds 1 3Fe-4S cluster.
Binds 1 4Fe-4S cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi64 – 641Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi67 – 671Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi79 – 791Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi150 – 1501Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi153 – 1531Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi156 – 1561Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi160 – 1601Iron-sulfur 3 (3Fe-4S) By similarity
Metal bindingi206 – 2061Iron-sulfur 3 (3Fe-4S) By similarity
Metal bindingi212 – 2121Iron-sulfur 3 (3Fe-4S) By similarity
Metal bindingi216 – 2161Iron-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
Complete GO annotation...

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

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate reductase iron-sulfur subunit (EC:1.3.5.1)
Gene namesi
Name:frdB
OrganismiProteus vulgaris
Taxonomic identifieri585 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 245244Fumarate reductase iron-sulfur subunit
PRO_0000158706Add
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.

Structurei

3D structure databases

ProteinModelPortaliP20921.
SMRiP20921. Positions 4-245.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 98862Fe-2S ferredoxin-type
Add
BLAST
Domaini141 – 170304Fe-4S ferredoxin-type
Add
BLAST

Sequence similaritiesi

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.

P20921-1 [UniParc]FASTAAdd to Basket

« Hide

MADDMKHVKM EVMRYNPETD DAPHFVTYDV PYDEQTSLLD ALGYIKDNLA    50
PDLSYRWSCR MAICGSCGMM VNRVPKLACK TFMRDYPNGV RIEALGNFPV 100
ERDLVVDMTH FIESLEAIKP YILGNDRKPS EGPNKQTPAQ MAKYHQFSGC 150
INCGLCYAAC PQFGLNPEFI GPAAITLAQR YNTDSRDHGA KERMPQLNGE 200
NGVWSCTFVG YCSEVCPKHV DPAAAIQQGK AASAQDFVIA MLKPR 245
Length:245
Mass (Da):27,331
Last modified:January 23, 2007 - v2
Checksum:iCEA17E28C8A390C2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06144 Genomic DNA. Translation: CAA29502.1.
PIRiS00108. RDEBIV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06144 Genomic DNA. Translation: CAA29502.1 .
PIRi S00108. RDEBIV.

3D structure databases

ProteinModelPortali P20921.
SMRi P20921. Positions 4-245.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris. Extensive sequence divergence of the membrane anchors and absence of an frd-linked ampC cephalosporinase gene."
    Cole S.T.
    Eur. J. Biochem. 167:481-488(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiFRDB_PROVU
AccessioniPrimary (citable) accession number: P20921
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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