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Protein

Fumarate reductase flavoprotein subunit

Gene

SO_0970

Organism
Shewanella oneidensis (strain MR-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi34Iron (heme 2 axial ligand)1
Binding sitei40Heme 1 (covalent)1
Binding sitei43Heme 1 (covalent)1
Metal bindingi44Iron (heme 1 axial ligand)1
Binding sitei63Heme 2 (covalent)1
Binding sitei66Heme 2 (covalent)1
Metal bindingi67Iron (heme 2 axial ligand)1
Metal bindingi85Iron (heme 3 axial ligand)1
Metal bindingi88Iron (heme 4 axial ligand)1
Binding sitei95Heme 3 (covalent)1
Binding sitei98Heme 3 (covalent)1
Metal bindingi99Iron (heme 3 axial ligand)1
Metal bindingi102Iron (heme 1 axial ligand)1
Binding sitei109Heme 4 (covalent)1
Binding sitei112Heme 4 (covalent)1
Metal bindingi113Iron (heme 4 axial ligand)1
Binding sitei389Substrate1 Publication1
Binding sitei401Substrate1 Publication1
Active sitei426Proton donorBy similarity1
Binding sitei528Substrate1 Publication1
Binding sitei569Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi156 – 167FAD1 PublicationAdd BLAST12
Nucleotide bindingi180 – 181FAD1 Publication2
Nucleotide bindingi187 – 189FAD1 Publication3
Nucleotide bindingi193 – 195FAD1 Publication3
Nucleotide bindingi572 – 575FAD1 Publication4

GO - Molecular functioni

  • electron carrier activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: GO_Central
  • succinate dehydrogenase activity Source: TIGR

GO - Biological processi

  • anaerobic respiration Source: TIGR
  • tricarboxylic acid cycle Source: TIGR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciSONE211586:GK2N-880-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate reductase flavoprotein subunit (EC:1.3.5.4)
Alternative name(s):
Flavocytochrome c
Short name:
FL cyt
Gene namesi
Ordered Locus Names:SO_0970
OrganismiShewanella oneidensis (strain MR-1)
Taxonomic identifieri211586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000008186 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB00518. Albendazole.
DB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25CuratedAdd BLAST25
ChainiPRO_000001034526 – 596Fumarate reductase flavoprotein subunitAdd BLAST571

Proteomic databases

PaxDbiP83223.

Expressioni

Inductioni

By anaerobiosis and fumarate.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi211586.SO_0970.

Structurei

Secondary structure

1596
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 33Combined sources4
Turni34 – 38Combined sources5
Turni41 – 43Combined sources3
Beta strandi44 – 48Combined sources5
Helixi57 – 67Combined sources11
Helixi70 – 76Combined sources7
Beta strandi79 – 81Combined sources3
Beta strandi86 – 88Combined sources3
Helixi95 – 97Combined sources3
Beta strandi101 – 103Combined sources3
Helixi108 – 111Combined sources4
Turni132 – 135Combined sources4
Helixi136 – 144Combined sources9
Beta strandi152 – 156Combined sources5
Helixi160 – 170Combined sources11
Beta strandi171 – 173Combined sources3
Beta strandi176 – 179Combined sources4
Beta strandi181 – 185Combined sources5
Helixi189 – 191Combined sources3
Beta strandi200 – 202Combined sources3
Helixi205 – 207Combined sources3
Helixi214 – 223Combined sources10
Turni224 – 226Combined sources3
Helixi230 – 238Combined sources9
Helixi240 – 249Combined sources10
Beta strandi256 – 258Combined sources3
Beta strandi268 – 271Combined sources4
Turni272 – 274Combined sources3
Helixi277 – 291Combined sources15
Beta strandi295 – 307Combined sources13
Beta strandi309 – 311Combined sources3
Beta strandi313 – 320Combined sources8
Turni321 – 323Combined sources3
Beta strandi324 – 329Combined sources6
Beta strandi331 – 335Combined sources5
Helixi344 – 350Combined sources7
Helixi352 – 354Combined sources3
Beta strandi359 – 361Combined sources3
Helixi368 – 375Combined sources8
Beta strandi386 – 393Combined sources8
Turni394 – 397Combined sources4
Helixi403 – 406Combined sources4
Beta strandi410 – 412Combined sources3
Helixi426 – 434Combined sources9
Helixi437 – 439Combined sources3
Beta strandi441 – 445Combined sources5
Helixi447 – 450Combined sources4
Helixi455 – 461Combined sources7
Beta strandi466 – 470Combined sources5
Helixi471 – 478Combined sources8
Helixi482 – 495Combined sources14
Turni502 – 504Combined sources3
Beta strandi515 – 530Combined sources16
Beta strandi533 – 536Combined sources4
Beta strandi541 – 556Combined sources16
Helixi558 – 560Combined sources3
Beta strandi561 – 563Combined sources3
Turni564 – 567Combined sources4
Helixi573 – 591Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D4CX-ray2.90A/B/C/D25-596[»]
1D4DX-ray2.50A25-596[»]
1D4EX-ray2.80A25-596[»]
ProteinModelPortaliP83223.
SMRiP83223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83223.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 141Cytochrome cAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni142 – 596Flavoprotein-likeAdd BLAST455

Sequence similaritiesi

In the C-terminal section; belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.Curated
Contains 1 cytochrome c domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107EFR. Bacteria.
COG1053. LUCA.
HOGENOMiHOG000227327.
KOiK00244.
OMAiGKMWENG.
OrthoDBiPOG091H02TE.
PhylomeDBiP83223.

Family and domain databases

Gene3Di1.10.1130.10. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR010960. Flavocytochrome_c.
IPR011031. Multihaem_cyt.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR012286. Tetrahaem_cytochrome.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
[Graphical view]
SUPFAMiSSF48695. SSF48695. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01813. flavo_cyto_c. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83223-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTRKIQKTA LAMLISGAMA GTAYAAPEVL ADFHGEMGGC DSCHVSDKGG
60 70 80 90 100
VTNDNLTHEN GQCVSCHGDL KELAAAAPKD KVSPHKSHLI GEIACTSCHK
110 120 130 140 150
GHEKSVAYCD ACHSFGFDMP FGGKWERKFV PVDADKAAQD KAIAAGVKET
160 170 180 190 200
TDVVIIGSGG AGLAAAVSAR DAGAKVILLE KEPIPGGNTK LAAGGMNAAE
210 220 230 240 250
TKPQAKLGIE DKKQIMIDDT MKGGRNINDP ELVKVLANNS SDSIDWLTSM
260 270 280 290 300
GADMTDVGRM GGASVNRSHR PTGGAGVGAH VAQVLWDNAV KRGTDIRLNS
310 320 330 340 350
RVVRILEDAS GKVTGVLVKG EYTGYYVIKA DAVVIAAGGF AKNNERVSKY
360 370 380 390 400
DPKLKGFKAT NHPGATGDGL DVALQAGAAT RDLEYIQAHP TYSPAGGVMI
410 420 430 440 450
TEAVRGNGAI VVNREGNRFM NEITTRDKAS AAILQQKGES AYLVFDDSIR
460 470 480 490 500
KSLKAIEGYV HLNIVKEGKT IEELAKQIDV PAAELAKTVT AYNGFVKSGK
510 520 530 540 550
DAQFERPDLP RELVVAPFYA LEIAPAVHHT MGGLVIDTKA EVKSEKTGKP
560 570 580 590
ITGLYAAGEV TGGVHGANRL GGNAISDIVT YGRIAGASAA KFAKDN
Length:596
Mass (Da):62,448
Last modified:November 25, 2002 - v2
Checksum:i74CB81FE89790463
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71K → E (PubMed:11425747).Curated1
Sequence conflicti282A → S (PubMed:11425747).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014299 Genomic DNA. Translation: AAN54044.1.
RefSeqiNP_716599.1. NC_004347.2.
WP_011071245.1. NC_004347.2.

Genome annotation databases

EnsemblBacteriaiAAN54044; AAN54044; SO_0970.
GeneIDi1168814.
KEGGison:SO_0970.
PATRICi23521593. VBISheOne101494_0930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014299 Genomic DNA. Translation: AAN54044.1.
RefSeqiNP_716599.1. NC_004347.2.
WP_011071245.1. NC_004347.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D4CX-ray2.90A/B/C/D25-596[»]
1D4DX-ray2.50A25-596[»]
1D4EX-ray2.80A25-596[»]
ProteinModelPortaliP83223.
SMRiP83223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi211586.SO_0970.

Chemistry databases

DrugBankiDB00518. Albendazole.
DB03147. Flavin adenine dinucleotide.

Proteomic databases

PaxDbiP83223.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN54044; AAN54044; SO_0970.
GeneIDi1168814.
KEGGison:SO_0970.
PATRICi23521593. VBISheOne101494_0930.

Phylogenomic databases

eggNOGiENOG4107EFR. Bacteria.
COG1053. LUCA.
HOGENOMiHOG000227327.
KOiK00244.
OMAiGKMWENG.
OrthoDBiPOG091H02TE.
PhylomeDBiP83223.

Enzyme and pathway databases

BioCyciSONE211586:GK2N-880-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP83223.

Family and domain databases

Gene3Di1.10.1130.10. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR010960. Flavocytochrome_c.
IPR011031. Multihaem_cyt.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR012286. Tetrahaem_cytochrome.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
[Graphical view]
SUPFAMiSSF48695. SSF48695. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01813. flavo_cyto_c. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFRDA_SHEON
AccessioniPrimary (citable) accession number: P83223
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: November 25, 2002
Last modified: November 30, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.