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 + acceptor = fumarate + reduced acceptor.
COFACTOR: Binds 1 2Fe-2S cluster (By similarity).
COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
SUBUNIT: Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins (By similarity).
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

AE014075; AAN83663.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_757089.1; -.

3D structure databases

SMR

P0AC48; 2-244.

ModBase

P0AC48.

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).

BLOCKS

P0AC48.

Genome annotation databases

GeneID

1037508; -.

GenomeReviews

AE014075_GR; c5241.

KEGG

ecc:c5241; -.

Phylogenomic databases

HOGENOM

P0AC48; -.

Genome annotation databases

CMR

P0AC48; c5241.

Other

ProtoNet

P0AC48.

UniRef

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

Keywords

2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; 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`	`2 244`	`243`	`Fumarate reductase iron-sulfur subunit.`	`PRO_0000158700`
`DOMAIN`	`16 97`	`82`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`140 169`	`30`	`4Fe-4S ferredoxin-type.`
`METAL`	`58 58`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`63 63`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`66 66`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`78 78`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`149 149`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`152 152`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`155 155`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`159 159`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`205 205`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`211 211`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`215 215`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`

Sequence information

Length: 244 AA [This is the length of the unprocessed precursor]

Molecular weight: 27123 Da [This is the MW of the unprocessed precursor]

CRC64: AC1D7A73244D7AC0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP DLSYRWSCRM 

        70         80         90        100        110        120 
AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY 

       130        140        150        160        170        180 
IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY 

       190        200        210        220        230        240 
NEDSRDHGKK ERMAQLNSQN GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT 


LKPR

P0AC48 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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