KEGG ENZYME: 1.3.2.4

ENZYME: 1.3.2.4

Entry

EC 1.3.2.4                  Enzyme

Name

fumarate reductase (cytochrome);
fccA (gene name);
fcc3 (gene name);
flavocytochrome c3

Class

Oxidoreductases;
Acting on the CH-CH group of donors;
With a cytochrome as acceptor

Sysname

succinate:ferricytochrome-c oxidoreductase

Reaction(IUBMB)

succinate + 2 ferricytochrome c = fumarate + 2 ferrocytochrome c [RN:R13137]

Reaction(KEGG)

R13137

Substrate

succinate [CPD:C00042];
ferricytochrome c [CPD:C00125]

Product

fumarate [CPD:C00122];
ferrocytochrome c [CPD:C00126]

Comment

Contains a non-covalently bound FAD cofactor and four heme c groups. The enzyme, characterized from the bacterium Shewanella frigidimarina, is a soluble periplasmic protein that functions as a terminal electron acceptor during anaerobic growth. The direct electron donor is the membrane-bound tetraheme c-type cytochrome CymA (EC 7.1.1.8, quinol---cytochrome-c reductase), which receives the electrons from the membrane quinol pool.

History

EC 1.3.2.4 created 2022

Pathway

ec00020

Citrate cycle (TCA cycle)

ec00620

Pyruvate metabolism

ec00650

Butanoate metabolism

ec00720

Carbon fixation pathways in prokaryotes

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

ec01120

Microbial metabolism in diverse environments

Orthology

K26318

fumarate reductase (cytochrome)

Genes

SON:	SO_0970(fccA)

SFR:

Sfri_3690

SAZ:

Sama_0611

SBL:

Sbal_0859

SBM:	Shew185_3505

SBN:	Sbal195_3628

SBP:	Sbal223_3433

SBT:	Sbal678_3651

SBS:	Sbal117_0955

SBB:	Sbal175_3411

SLO:

Shew_3112

SPC:	Sputcn32_0905

SHP:	Sput200_0902

SSE:

Ssed_3877

SPL:

Spea_0722

SHE:	Shewmr4_0808

SHM:	Shewmr7_3215

SHN:	Shewana3_3318

SHW:	Sputw3181_3267

SHL:

Shal_0776

SWD:

Swoo_3776

SWP:

swp_4352

SHF:	CEQ32_11620

SJA:	SJ2017_0503

SPSW:

Sps_04949

SBJ:	CF168_04200

SMAV:

CFF01_15645

SHEW:

CKQ84_03180

SALG:

BS332_03245

SLJ:	EGC82_20545

SMAI:

EXU30_11795

SPOL:

FH971_18500

SBK:	SHEWBE_1282(fccA)

SKH:	STH12_00145

SLIT:

JQC75_02835

SCAA:

TUM17387_07670

SPSH:

FM037_23565

SEUR:

FM038_004020

SYK:	KDN34_13800

SAVI:

JYB87_03940

SGLA:

FJ709_02680

SINV:

K8B83_04405

SXM:	MKD32_16500(fccA)

SVM:	KDH10_003463

SHEJ:

MZ182_04200(fccA)

SSEH:

N7V09_06640(fccA)

SCHK:

GII14_18165

SACH:

K0H61_13985(fccA)

SAEG:

K0H80_15945

SDEO:

D0436_17960(fccA)

SMES:

K0I73_03760

SHAO:

K0H81_16235

SZH:	K0H63_03445(fccA)

SSPA:

K0I31_16180

SHNS:

K0J45_15960

SRHS:

K0I63_16090

SPSJ:

K0I62_03605

SMAY:

K0H60_16630(fccA)

SOG:	RA178_17680(fccA)

SPSR:

EGC80_06710

FBL:

Fbal_1806

FES:	HER31_12130

GEM:

GM21_4127

GEB:

GM18_3822

GEF:	FO488_03675

GLO:	Glov_3541 Glov_3625

GBM:	Gbem_3597 Gbem_4036

GBN:	GEOBRER4_39050

GER:	KP004_01890 KP004_19445

GSUB:

KP001_13600 KP001_16875

GNT:	KP003_01525 KP003_19430

GPL:	M1B72_00310 M1B72_19080

GEP:	Q9293_09155

MSIL:

METEAL_10940

MSEA:

METESE_16190

MSCH:

N508_000493

» show all

Reference

1 [PMID:1333793]

Authors

Pealing SL, Black AC, Manson FD, Ward FB, Chapman SK, Reid GA.

Title

Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria.

Journal

Biochemistry 31:12132-40 (1992)
DOI:10.1021/bi00163a023

Sequence

[sfr:Sfri_3690]

Reference

2 [PMID:7742319]

Authors

Pealing SL, Cheesman MR, Reid GA, Thomson AJ, Ward FB, Chapman SK.

Title

Spectroscopic and kinetic studies of the tetraheme flavocytochrome c from Shewanella putrefaciens NCIMB400.

Journal

Biochemistry 34:6153-8 (1995)
DOI:10.1021/bi00018a018

Reference

3 [PMID:9579067]

Authors

Gordon EHJ, Pealing SL, Chapman SK, Ward FB, Reid GA.

Title

Physiological function and regulation of flavocytochrome c3, the soluble fumarate reductase from Shewanella putrefaciens NCIMB 400.

Journal

Microbiology (Reading) 144 ( Pt 4):937-945 (1998)
DOI:10.1099/00221287-144-4-937

Reference

4 [PMID:10978153]

Authors

Doherty MK, Pealing SL, Miles CS, Moysey R, Taylor P, Walkinshaw MD, Reid GA, Chapman SK.

Title

Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study.

Journal

Biochemistry 39:10695-701 (2000)
DOI:10.1021/bi000871l

Reference

5 [PMID:11004445]

Authors

Reid GA, Miles CS, Moysey RK, Pankhurst KL, Chapman SK.

Title

Catalysis in fumarate reductase.

Journal

Biochim Biophys Acta 1459:310-5 (2000)
DOI:10.1016/s0005-2728(00)00166-3

Sequence

[son:SO_0970] [sfr:Sfri_3690]

Reference

6 [PMID:12196158]

Authors

Schwalb C, Chapman SK, Reid GA.

Title

The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella.

Journal

Biochem Soc Trans 30:658-62 (2002)
DOI:10.1042/bst0300658

Other DBs

ExplorEnz - The Enzyme Database:

1.3.2.4

IUBMB Enzyme Nomenclature:

1.3.2.4

ExPASy - ENZYME nomenclature database:

1.3.2.4

BRENDA, the Enzyme Database:

1.3.2.4

All links

Pathway (14)   
   KEGG PATHWAY (14)   
Chemical substance (4)   
   KEGG COMPOUND (4)   
Chemical reaction (2)   
   KEGG REACTION (1)   
   KEGG RCLASS (1)   
Gene (169)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (82)   
   KEGG MGENES (86)   
All databases (189)   

Download RDF

DBGET integrated database retrieval system