[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00276536; PubMed=2244791 [NCBI, ExPASy, EBI, Israel, Japan] Lauterbach F., Koertner C., Albracht S.P., Unden G., Kroeger A.; "The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes."; Arch. Microbiol. 154:386-393(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. PubMed=9492313 [NCBI, ExPASy, EBI, Israel, Japan] Simon J., Gross R., Ringel M., Schmidt E., Kroeger A.; "Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon."; Eur. J. Biochem. 251:418-426(1998).
[3]	SEQUENCE REVISION TO 281-289; 490 AND 593. Simon J.; Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=DSMZ 1740; DOI=10.1073/pnas.1932838100; PubMed=14500908 [NCBI, ExPASy, EBI, Israel, Japan] Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C.; "Complete genome sequence and analysis of Wolinella succinogenes."; Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25. PubMed=3609021 [NCBI, ExPASy, EBI, Israel, Japan] Lauterbach F., Kortner C., Tripier D., Unden G.; "Cloning and expression of the genes of two fumarate reductase subunits from Wolinella succinogenes."; Eur. J. Biochem. 166:447-452(1987).
[6]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SEQUENCE REVISION TO 281-289. DOI=10.1038/46483; PubMed=10586875 [NCBI, ExPASy, EBI, Israel, Japan] Lancaster C.R.D., Kroeger A., Auer M., Michel H.; "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution."; Nature 402:377-385(1999).
[7]	X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). PubMed=11248702 [NCBI, ExPASy, EBI, Israel, Japan] Lancaster C.R.D., Gross R., Simon J.; "A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction."; Eur. J. Biochem. 268:1820-1827(2001).

Comments

FUNCTION: The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
CATALYTIC ACTIVITY: Succinate + acceptor = fumarate + reduced acceptor.
COFACTOR: Binds 1 FAD covalently per subunit.
SUBUNIT: Part of an enzyme complex containing three subunits: a flavoprotein, an iron-sulfur protein, and cytochrome b-556.
SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

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

AJ000662; CAA04214.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX571659; CAE09942.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M28294; AAA27586.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B44954; B44954.

RefSeq

NP_907042.1; -.

3D structure databases

PDB

1E7P; X-ray; 3.10 A; A/D=1-656, G/J=1-655.	[ExPASy / RCSB / EBI]
1QLB; X-ray; 2.33 A; A/D=1-656.	[ExPASy / RCSB / EBI]
2BS2; X-ray; 1.78 A; A/D=1-656.	[ExPASy / RCSB / EBI]
2BS3; X-ray; 2.19 A; A/D=1-656.	[ExPASy / RCSB / EBI]
2BS4; X-ray; 2.76 A; A/D=1-656.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1E7P; -.
1QLB; -.
2BS2; -.
2BS3; -.
2BS4; -.

ModBase

P17412.

Enzyme and pathway databases

BioCyc

WSUC273121:WS0831-MON; -.

Family and domain databases

InterPro

IPR003953; FAD_bind2_N.
IPR003952; FRD_SDH_FAD_BS.
IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
IPR014006; Succ_Dhase_frdA_Gneg.
Graphical view of domain structure.

Pfam

PF00890; FAD_binding_2; 1.
PF02910; Succ_DH_flav_C; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01812; sdhA_frdA_Gneg; 1.

PROSITE

PS00504; FRD_SDH_FAD_BINDING; 1.

BLOCKS

P17412.

Genome annotation databases

2555184; -.

BX571656_GR; WS0831.

wsu:WS0831; -.

fig|273121.1.peg.769; -.

Phylogenomic databases

HOGENOM

P17412; -.

Genome annotation databases

CMR

P17412; WS0831.

Other

ProtoNet

P17412.

UniRef

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

Keywords

3D-structure; Complete proteome; Electron transport; FAD; Flavoprotein; Oxidoreductase; Respiratory chain; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 656`	`656`	`Fumarate reductase flavoprotein subunit.`	`PRO_0000158667`
`NP_BIND`	`9 23`	`15`	`FAD (Potential).`
`ACT_SITE`	`257 257`		`By similarity.`
`ACT_SITE`	`273 273`		`By similarity.`
`MOD_RES`	`43 43`		`Tele-8alpha-FAD histidine.`
`STRAND`	`3 11`	`9`
`HELIX`	`15 25`	`11`
`TURN`	`26 28`	`3`
`STRAND`	`31 34`	`4`
`HELIX`	`39 41`	`3`
`HELIX`	`43 46`	`4`
`HELIX`	`59 61`	`3`
`HELIX`	`66 76`	`11`
`TURN`	`77 79`	`3`
`HELIX`	`83 102`	`20`
`STRAND`	`112 115`	`4`
`STRAND`	`119 122`	`4`
`STRAND`	`126 128`	`3`
`HELIX`	`130 132`	`3`
`HELIX`	`156 171`	`16`
`STRAND`	`174 176`	`3`
`STRAND`	`178 187`	`10`
`STRAND`	`190 198`	`9`
`TURN`	`199 201`	`3`
`STRAND`	`204 214`	`11`
`HELIX`	`220 222`	`3`
`STRAND`	`223 228`	`6`
`HELIX`	`235 241`	`7`
`STRAND`	`244 246`	`3`
`STRAND`	`254 258`	`5`
`TURN`	`262 264`	`3`
`TURN`	`270 272`	`3`
`STRAND`	`273 275`	`3`
`STRAND`	`278 280`	`3`
`HELIX`	`288 291`	`4`
`TURN`	`293 295`	`3`
`HELIX`	`296 298`	`3`
`HELIX`	`301 313`	`13`
`TURN`	`314 316`	`3`
`STRAND`	`325 329`	`5`
`TURN`	`331 333`	`3`
`HELIX`	`345 351`	`7`
`TURN`	`357 359`	`3`
`STRAND`	`362 364`	`3`
`STRAND`	`367 371`	`5`
`STRAND`	`374 376`	`3`
`STRAND`	`384 386`	`3`
`STRAND`	`388 390`	`3`
`HELIX`	`392 394`	`3`
`HELIX`	`408 430`	`23`
`STRAND`	`434 436`	`3`
`HELIX`	`437 456`	`20`
`HELIX`	`463 477`	`15`
`STRAND`	`478 482`	`5`
`HELIX`	`484 501`	`18`
`STRAND`	`511 513`	`3`
`HELIX`	`515 539`	`25`
`STRAND`	`554 556`	`3`
`TURN`	`557 559`	`3`
`STRAND`	`562 567`	`6`
`STRAND`	`577 582`	`6`
`HELIX`	`585 587`	`3`
`STRAND`	`596 601`	`6`
`HELIX`	`607 625`	`19`
`HELIX`	`630 637`	`8`
`HELIX`	`644 646`	`3`

Sequence information

Length: 656 AA [This is the length of the unprocessed precursor]

Molecular weight: 72719 Da [This is the MW of the unprocessed precursor]

CRC64: BFEE6E8316F7F618 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVQYCDSLV IGGGLAGLRA AVATQQKGLS TIVLSLIPVK RSHSAAAQGG MQASLGNSKM 

        70         80         90        100        110        120 
SDGDNEDLHF MDTVKGSDWG CDQKVARMFV NTAPKAIREL AAWGVPWTRI HKGDRMAIIN 

       130        140        150        160        170        180 
AQKTTITEED FRHGLIHSRD FGGTKKWRTC YTADATGHTM LFAVANECLK LGVSIQDRKE 

       190        200        210        220        230        240 
AIALIHQDGK CYGAVVRDLV TGDIIAYVAK GTLIATGGYG RIYKNTTNAV VCEGTGTAIA 

       250        260        270        280        290        300 
LETGIAQLGN MEAVQFHPTP LFPSGILLTE GCRGDGGILR DVDGHRFMPD YEPEKKELAS 

       310        320        330        340        350        360 
RDVVSRRMIE HIRKGKGVQS PYGQHLWLDI SILGRKHIET NLRDVQEICE YFAGIDPAEK 

       370        380        390        400        410        420 
WAPVLPMQHY SMGGIRTDYR GEAKLKGLFS AGEAACWDMH GFNRLGGNSV SEAVVAGMIV 

       430        440        450        460        470        480 
GEYFAEHCAN TQVDLETKTL EKFVKGQEAY MKSLVESKGT EDVFKIKNRM KDVMDDNVGI 

       490        500        510        520        530        540 
FRDGPHLEKA VKELEELYKK SKNVGIKNKR LHANPELEEA YRVPMMLKVA LCVAKGALDR 

       550        560        570        580        590        600 
TESRGAHNRE DYPKRDDINW LNRTLASWPN PEQTLPTLEY EALDVNEMEI APGYRGYGAK 

       610        620        630        640        650 
GNYIENPLSV KRQEEIDKIQ SELEAAGKDR HAIQEALMPY ELPAKYKARN ERLGDK

P17412 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