Reviewed, UniProtKB/Swiss-Prot P83223 (FRDA_SHEON)

Names and origin

Protein names

Recommended name:
    Fumarate reductase flavoprotein subunit
    EC=1.3.99.1
Alternative name(s):
    Flavocytochrome c
      Short name=FL cyt

Gene names

Ordered Locus Names:

SO_0970

Organism

Shewanella oneidensis [Complete proteome] [HAMAP]

Taxonomic identifier

70863 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	596 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional By similarity.
Catalytic activity	Succinate + acceptor = fumarate + reduced acceptor.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Monomer.
Subcellular location	Periplasm By similarity.
Induction	By anaerobiosis and fumarate. Ref.1
Sequence similarities	In the C-terminal section; belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. Contains 1 cytochrome c domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	FAD Flavoprotein Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Probable

Chain

26 – 596

571

Fumarate reductase flavoprotein subunit

PRO_0000010345

Regions

Domain

26 – 141

116

Cytochrome c

Nucleotide binding

156 – 167

12

FAD

Nucleotide binding

180 – 181

2

FAD

Nucleotide binding

187 – 189

3

FAD

Nucleotide binding

193 – 195

3

FAD

Nucleotide binding

572 – 575

4

FAD

Region

142 – 596

455

Flavoprotein-like

Sites

Active site

426

1

Proton donor By similarity

Metal binding

34

1

Iron (heme 2 axial ligand)

Metal binding

44

1

Iron (heme 1 axial ligand)

Metal binding

67

1

Iron (heme 2 axial ligand)

Metal binding

85

1

Iron (heme 3 axial ligand)

Metal binding

88

1

Iron (heme 4 axial ligand)

Metal binding

99

1

Iron (heme 3 axial ligand)

Metal binding

102

1

Iron (heme 1 axial ligand)

Metal binding

113

1

Iron (heme 4 axial ligand)

Binding site

40

1

Heme 1 (covalent)

Binding site

43

1

Heme 1 (covalent)

Binding site

63

1

Heme 2 (covalent)

Binding site

66

1

Heme 2 (covalent)

Binding site

95

1

Heme 3 (covalent)

Binding site

98

1

Heme 3 (covalent)

Binding site

109

1

Heme 4 (covalent)

Binding site

112

1

Heme 4 (covalent)

Binding site

389

1

Substrate

Binding site

401

1

Substrate

Binding site

528

1

Substrate

Binding site

569

1

Substrate

Experimental info

Sequence conflict

71

1

K → E Ref.1

Sequence conflict

282

1

A → S Ref.1

Secondary structure

1

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596

Helix Strand Turn

Details...

Helix

30 – 38

9

Turn

41 – 43

3

Beta strand

44 – 46

3

Helix

57 – 67

11

Helix

70 – 75

6

Beta strand

79 – 81

3

Helix

95 – 97

3

Beta strand

101 – 103

3

Helix

108 – 111

4

Turn

132 – 135

4

Helix

136 – 144

9

Beta strand

152 – 156

5

Helix

160 – 170

11

Turn

171 – 173

3

Beta strand

176 – 179

4

Beta strand

181 – 185

5

Helix

189 – 191

3

Helix

202 – 206

5

Helix

213 – 223

11

Turn

224 – 226

3

Helix

230 – 238

9

Helix

240 – 249

10

Beta strand

256 – 258

3

Beta strand

268 – 271

4

Turn

272 – 274

3

Helix

278 – 291

14

Beta strand

295 – 297

3

Beta strand

300 – 306

7

Beta strand

309 – 311

3

Beta strand

315 – 320

6

Turn

321 – 323

3

Beta strand

324 – 329

6

Beta strand

331 – 335

5

Helix

344 – 350

7

Helix

352 – 354

3

Helix

368 – 375

8

Beta strand

386 – 393

8

Turn

394 – 397

4

Helix

403 – 406

4

Beta strand

410 – 412

3

Helix

426 – 434

9

Beta strand

441 – 446

6

Helix

447 – 451

5

Helix

456 – 461

6

Beta strand

466 – 470

5

Helix

471 – 478

8

Helix

482 – 498

17

Beta strand

502 – 504

3

Beta strand

515 – 530

16

Beta strand

541 – 544

4

Turn

545 – 547

3

Beta strand

548 – 556

9

Helix

558 – 560

3

Beta strand

563 – 565

3

Helix

573 – 594

22

Sequences

	Sequence		Length	Mass (Da)
	P83223-1 [UniParc]. Last modified November 25, 2002. Version 2. Checksum: 74CB81FE89790463	FASTA	596	62,448
	10 20 30 40 50 60 MFTRKIQKTA LAMLISGAMA GTAYAAPEVL ADFHGEMGGC DSCHVSDKGG VTNDNLTHEN 70 80 90 100 110 120 GQCVSCHGDL KELAAAAPKD KVSPHKSHLI GEIACTSCHK GHEKSVAYCD ACHSFGFDMP 130 140 150 160 170 180 FGGKWERKFV PVDADKAAQD KAIAAGVKET TDVVIIGSGG AGLAAAVSAR DAGAKVILLE 190 200 210 220 230 240 KEPIPGGNTK LAAGGMNAAE TKPQAKLGIE DKKQIMIDDT MKGGRNINDP ELVKVLANNS 250 260 270 280 290 300 SDSIDWLTSM GADMTDVGRM GGASVNRSHR PTGGAGVGAH VAQVLWDNAV KRGTDIRLNS 310 320 330 340 350 360 RVVRILEDAS GKVTGVLVKG EYTGYYVIKA DAVVIAAGGF AKNNERVSKY DPKLKGFKAT 370 380 390 400 410 420 NHPGATGDGL DVALQAGAAT RDLEYIQAHP TYSPAGGVMI TEAVRGNGAI VVNREGNRFM 430 440 450 460 470 480 NEITTRDKAS AAILQQKGES AYLVFDDSIR KSLKAIEGYV HLNIVKEGKT IEELAKQIDV 490 500 510 520 530 540 PAAELAKTVT AYNGFVKSGK DAQFERPDLP RELVVAPFYA LEIAPAVHHT MGGLVIDTKA 550 560 570 580 590 EVKSEKTGKP ITGLYAAGEV TGGVHGANRL GGNAISDIVT YGRIAGASAA KFAKDN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1." Tsapin A.I., Vandenberghe I., Nealson K.H., Scott J.H., Meyer T.E., Cusanovich M.A., Harada E., Kaizu T., Akutsu H., Leys D., Van Beeumen J.J. Appl. Environ. Microbiol. 67:3236-3244(2001) [PubMed: 11425747] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: MR-1.
[2]	"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis." Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T. , Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M. Nat. Biotechnol. 20:1118-1123(2002) [PubMed: 12368813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MR-1.
[3]	"Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1." Leys D., Tsapin A.S., Nealson K.H., Meyer T.E., Cusanovich M.A., Van Beeumen J.J. Nat. Struct. Biol. 6:1113-1117(1999) [PubMed: 10581551] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FAD; HEMES AND SUBSTRATE. Strain: MR-1.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE014299 Genomic DNA. Translation: AAN54044.1.

RefSeq

NP_716599.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D4C	X-ray	2.90	A/B/C/D	25-596	[»]
1D4D	X-ray	2.50	A	25-596	[»]
1D4E	X-ray	2.80	A	25-596	[»]

ModBase

Search...

Genome annotation databases

GeneID

1168814.

GenomeReviews

Gene locus SO_0970 in contig AE014299_GR.

KEGG

son:SO_0970.

NMPDR

fig|211586.1.peg.905.

TIGR

SO_0970.

Phylogenomic databases

HOGENOM

P83223.

OMA

P83223. YIQAHPT.

Enzyme and pathway databases

BioCyc

SONE211586:SO_0970-MON.

BRENDA

1.3.99.1. 257422.

Family and domain databases

InterPro

IPR003953. FAD_bind2_N.
IPR012286. FlavoCyt_c3_N.
IPR010960. Flavocytochrome_c.
IPR011031. Multihaem_cyt.
[Graphical view]

Gene3D

G3DSA:1.10.1130.10. Fcc3_N_cyt. 1 hit.

Pfam

PF00890. FAD_binding_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01813. flavo_cyto_c. 1 hit.

PROSITE

PS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FRDA_SHEON

Accession

Primary (citable) accession number: P83223

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	November 25, 2002
Last modified:	June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)