Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fumarate reductase iron-sulfur subunit

Gene

frdB

Organism
Proteus vulgaris
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi64Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi67Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi79Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi150Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi153Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi156Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi160Iron-sulfur 3 (3Fe-4S)By similarity1
Metal bindingi206Iron-sulfur 3 (3Fe-4S)By similarity1
Metal bindingi212Iron-sulfur 3 (3Fe-4S)By similarity1
Metal bindingi216Iron-sulfur 2 (4Fe-4S)By similarity1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001587062 – 245Fumarate reductase iron-sulfur subunitAdd BLAST244

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 982Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST86
Domaini141 – 1704Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST30

Sequence similaritiesi

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

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

        10         20         30         40         50
MADDMKHVKM EVMRYNPETD DAPHFVTYDV PYDEQTSLLD ALGYIKDNLA
60 70 80 90 100
PDLSYRWSCR MAICGSCGMM VNRVPKLACK TFMRDYPNGV RIEALGNFPV
110 120 130 140 150
ERDLVVDMTH FIESLEAIKP YILGNDRKPS EGPNKQTPAQ MAKYHQFSGC
160 170 180 190 200
INCGLCYAAC PQFGLNPEFI GPAAITLAQR YNTDSRDHGA KERMPQLNGE
210 220 230 240
NGVWSCTFVG YCSEVCPKHV DPAAAIQQGK AASAQDFVIA MLKPR
Length:245
Mass (Da):27,331
Last modified:January 23, 2007 - v2
Checksum:iCEA17E28C8A390C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06144 Genomic DNA. Translation: CAA29502.1.
PIRiS00108. RDEBIV.
RefSeqiWP_004248868.1. NZ_CP012675.1.

Genome annotation databases

GeneIDi6801672.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06144 Genomic DNA. Translation: CAA29502.1.
PIRiS00108. RDEBIV.
RefSeqiWP_004248868.1. NZ_CP012675.1.

3D structure databases

ProteinModelPortaliP20921.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6801672.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 93 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.