NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3308458 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T.;
"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.";
Eur. J. Biochem. 167:481-488(1987).

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.
CATALYTIC ACTIVITY: Succinate + acceptor = fumarate + reduced acceptor.
COFACTOR: Binds 1 2Fe-2S cluster.
COFACTOR: Binds 1 3Fe-4S cluster.
COFACTOR: Binds 1 4Fe-4S cluster.
SUBUNIT: Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins.
SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.

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

X06144; CAA29502.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S00108; RDEBIV.

3D structure databases

HSSP

P00364; 1KF6. [HSSP ENTRY / PDB]

SMR

P20921; 4-245.

ModBase

P20921.

Ontologies

GO:0000104;	Molecular function: succinate dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR006058; 2Fe2S_fd_BS.
IPR001450; 4Fe4S_Fe_S_bd.
IPR012675; b-grasp_ferredoxin-like.
IPR001041; Ferredoxin.
IPR012285; Fum_reductase_C.
IPR004489; Succ_DHase/fum_Rdtase_Fe-S.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.20.30; Ferredoxin_fold; 1.
G3DSA:1.10.1060.10; Fum_reductase_C; 1.

Pfam

PF00111; Fer2; 1.
PF00037; Fer4; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00384; dhsB; 1.

PROSITE

PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS00198; 4FE4S_FER_1; 1.
PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

2Fe-2S; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Transport; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 245`	`244`	`Fumarate reductase iron-sulfur subunit.`	`PRO_0000158706`
`DOMAIN`	`13 98`	`86`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`141 170`	`30`	`4Fe-4S ferredoxin-type.`
`METAL`	`59 59`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`64 64`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`67 67`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`79 79`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`150 150`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`153 153`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`156 156`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`160 160`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`206 206`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`212 212`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`216 216`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`

Sequence information

Length: 245 AA [This is the length of the unprocessed precursor]

Molecular weight: 27331 Da [This is the MW of the unprocessed precursor]

CRC64: CEA17E28C8A390C2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADDMKHVKM EVMRYNPETD DAPHFVTYDV PYDEQTSLLD ALGYIKDNLA PDLSYRWSCR 

        70         80         90        100        110        120 
MAICGSCGMM VNRVPKLACK TFMRDYPNGV RIEALGNFPV ERDLVVDMTH FIESLEAIKP 

       130        140        150        160        170        180 
YILGNDRKPS EGPNKQTPAQ MAKYHQFSGC INCGLCYAAC PQFGLNPEFI GPAAITLAQR 

       190        200        210        220        230        240 
YNTDSRDHGA KERMPQLNGE NGVWSCTFVG YCSEVCPKHV DPAAAIQQGK AASAQDFVIA 


MLKPR

P20921 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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