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P83223

- FRDA_SHEON

UniProt

P83223 - FRDA_SHEON

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Protein

Fumarate reductase flavoprotein subunit

Gene

SO_0970

Organism
Shewanella oneidensis (strain MR-1)
Status
Reviewed - 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

Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Iron (heme 2 axial ligand)
Binding sitei40 – 401Heme 1 (covalent)
Binding sitei43 – 431Heme 1 (covalent)
Metal bindingi44 – 441Iron (heme 1 axial ligand)
Binding sitei63 – 631Heme 2 (covalent)
Binding sitei66 – 661Heme 2 (covalent)
Metal bindingi67 – 671Iron (heme 2 axial ligand)
Metal bindingi85 – 851Iron (heme 3 axial ligand)
Metal bindingi88 – 881Iron (heme 4 axial ligand)
Binding sitei95 – 951Heme 3 (covalent)
Binding sitei98 – 981Heme 3 (covalent)
Metal bindingi99 – 991Iron (heme 3 axial ligand)
Metal bindingi102 – 1021Iron (heme 1 axial ligand)
Binding sitei109 – 1091Heme 4 (covalent)
Binding sitei112 – 1121Heme 4 (covalent)
Metal bindingi113 – 1131Iron (heme 4 axial ligand)
Binding sitei389 – 3891Substrate1 Publication
Binding sitei401 – 4011Substrate1 Publication
Active sitei426 – 4261Proton donorBy similarity
Binding sitei528 – 5281Substrate1 Publication
Binding sitei569 – 5691Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi156 – 16712FAD1 PublicationAdd
BLAST
Nucleotide bindingi180 – 1812FAD1 Publication
Nucleotide bindingi187 – 1893FAD1 Publication
Nucleotide bindingi193 – 1953FAD1 Publication
Nucleotide bindingi572 – 5754FAD1 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. succinate dehydrogenase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding

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
ProteomesiUP000008186: Chromosome

Subcellular locationi

Periplasm By similarity

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525CuratedAdd
BLAST
Chaini26 – 596571Fumarate reductase flavoprotein subunitPRO_0000010345Add
BLAST

Expressioni

Inductioni

By anaerobiosis and fumarate.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi211586.SO_0970.

Structurei

Secondary structure

1
596
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 334
Turni34 – 385
Turni41 – 433
Beta strandi44 – 485
Helixi57 – 6711
Helixi70 – 767
Beta strandi79 – 813
Beta strandi86 – 883
Helixi95 – 973
Beta strandi101 – 1033
Helixi108 – 1114
Turni132 – 1354
Helixi136 – 1449
Beta strandi152 – 1565
Helixi160 – 17011
Beta strandi171 – 1733
Beta strandi176 – 1794
Beta strandi181 – 1855
Helixi189 – 1913
Beta strandi200 – 2023
Helixi205 – 2073
Helixi214 – 22310
Turni224 – 2263
Helixi230 – 2389
Helixi240 – 24910
Beta strandi256 – 2583
Beta strandi268 – 2714
Turni272 – 2743
Helixi277 – 29115
Beta strandi295 – 30713
Beta strandi309 – 3113
Beta strandi313 – 3208
Turni321 – 3233
Beta strandi324 – 3296
Beta strandi331 – 3355
Helixi344 – 3507
Helixi352 – 3543
Beta strandi359 – 3613
Helixi368 – 3758
Beta strandi386 – 3938
Turni394 – 3974
Helixi403 – 4064
Beta strandi410 – 4123
Helixi426 – 4349
Helixi437 – 4393
Beta strandi441 – 4455
Helixi447 – 4504
Helixi455 – 4617
Beta strandi466 – 4705
Helixi471 – 4788
Helixi482 – 49514
Turni502 – 5043
Beta strandi515 – 53016
Beta strandi533 – 5364
Beta strandi541 – 55616
Helixi558 – 5603
Beta strandi561 – 5633
Turni564 – 5674
Helixi573 – 59119

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D4CX-ray2.90A/B/C/D25-596[»]
1D4DX-ray2.50A25-596[»]
1D4EX-ray2.80A25-596[»]
ProteinModelPortaliP83223.
SMRiP83223. Positions 26-595.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83223.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 141116Cytochrome cAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 596455Flavoprotein-likeAdd
BLAST

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

eggNOGiCOG1053.
HOGENOMiHOG000227327.
KOiK00244.
OMAiCDSCHSF.
OrthoDBiEOG6XHC2W.
PhylomeDBiP83223.

Family and domain databases

Gene3Di1.10.1130.10. 1 hit.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD_bind_dom.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
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]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF56425. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711K → E(PubMed:11425747)Curated
Sequence conflicti282 – 2821A → S(PubMed:11425747)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE014299 Genomic DNA. Translation: AAN54044.1 .
RefSeqi NP_716599.1. NC_004347.2.
WP_011071245.1. NC_004347.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P83223.
SMRi P83223. Positions 26-595.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 211586.SO_0970.

Chemistry

DrugBanki DB00518. Albendazole.
DB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN54044 ; AAN54044 ; SO_0970 .
GeneIDi 1168814.
KEGGi son:SO_0970.
PATRICi 23521593. VBISheOne101494_0930.

Phylogenomic databases

eggNOGi COG1053.
HOGENOMi HOG000227327.
KOi K00244.
OMAi CDSCHSF.
OrthoDBi EOG6XHC2W.
PhylomeDBi P83223.

Miscellaneous databases

EvolutionaryTracei P83223.

Family and domain databases

Gene3Di 1.10.1130.10. 1 hit.
3.90.700.10. 1 hit.
InterProi IPR003953. FAD_bind_dom.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR010960. Flavocytochrome_c.
IPR011031. Multihaem_cyt.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR012286. Tetrahaem_cytochrome.
[Graphical view ]
Pfami PF00890. FAD_binding_2. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF56425. SSF56425. 1 hit.
TIGRFAMsi TIGR01813. flavo_cyto_c. 1 hit.
PROSITEi PS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: MR-1.
  2. 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FAD; HEMES AND SUBSTRATE.
    Strain: MR-1.

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: October 29, 2014
This is version 105 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

External Data

Dasty 3