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Protein

Fumarate reductase flavoprotein subunit

Gene

ifcA

Organism
Shewanella frigidimarina (strain NCIMB 400)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes unidirectional fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown.

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi31Iron (heme 2 axial ligand)1
Binding sitei37Heme 1 (covalent)1
Binding sitei40Heme 1 (covalent)1
Metal bindingi41Iron (heme 1 axial ligand)1
Binding sitei58Heme 2 (covalent)1
Binding sitei61Heme 2 (covalent)1
Metal bindingi62Iron (heme 2 axial ligand)1
Metal bindingi78Iron (heme 3 axial ligand)1
Metal bindingi81Iron (heme 4 axial ligand)1
Binding sitei87Heme 3 (covalent)1
Binding sitei90Heme 3 (covalent)1
Metal bindingi91Iron (heme 3 axial ligand)1
Metal bindingi94Iron (heme 1 axial ligand)1
Binding sitei101Heme 4 (covalent)1
Binding sitei104Heme 4 (covalent)1
Metal bindingi105Iron (heme 4 axial ligand)1
Active sitei382By similarity1
Active sitei398By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi146 – 160FADSequence analysisAdd BLAST15

GO - Molecular functioni

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):
Fe(3+)-induced flavocytochrome C3
Short name:
Ifc3
Iron(III)-induced flavocytochrome C3
Gene namesi
Name:ifcA
Ordered Locus Names:Sfri_2586
OrganismiShewanella frigidimarina (strain NCIMB 400)
Taxonomic identifieri318167 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000000684 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000001034623 – 588Fumarate reductase flavoprotein subunitAdd BLAST566

Proteomic databases

PRIDEiQ9Z4P0.

Expressioni

Inductioni

By anaerobic growth on Fe3+ ions.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi318167.Sfri_2586.

Structurei

Secondary structure

1588
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 34Combined sources8
Helixi37 – 39Combined sources3
Helixi52 – 62Combined sources11
Helixi65 – 68Combined sources4
Beta strandi71 – 75Combined sources5
Helixi87 – 89Combined sources3
Beta strandi93 – 95Combined sources3
Helixi100 – 103Combined sources4
Turni113 – 116Combined sources4
Helixi129 – 137Combined sources9
Beta strandi141 – 149Combined sources9
Helixi153 – 165Combined sources13
Beta strandi169 – 172Combined sources4
Beta strandi174 – 178Combined sources5
Helixi182 – 184Combined sources3
Helixi195 – 199Combined sources5
Helixi206 – 216Combined sources11
Turni217 – 219Combined sources3
Helixi223 – 242Combined sources20
Beta strandi249 – 251Combined sources3
Beta strandi261 – 263Combined sources3
Beta strandi265 – 268Combined sources4
Helixi270 – 284Combined sources15
Beta strandi292 – 300Combined sources9
Beta strandi304 – 313Combined sources10
Turni314 – 316Combined sources3
Beta strandi317 – 328Combined sources12
Helixi337 – 343Combined sources7
Helixi345 – 347Combined sources3
Helixi361 – 368Combined sources8
Beta strandi373 – 375Combined sources3
Beta strandi379 – 389Combined sources11
Helixi396 – 399Combined sources4
Beta strandi403 – 405Combined sources3
Helixi419 – 427Combined sources9
Helixi430 – 432Combined sources3
Beta strandi434 – 439Combined sources6
Helixi440 – 445Combined sources6
Helixi447 – 454Combined sources8
Beta strandi459 – 463Combined sources5
Helixi464 – 470Combined sources7
Helixi475 – 491Combined sources17
Turni495 – 497Combined sources3
Beta strandi508 – 523Combined sources16
Beta strandi534 – 537Combined sources4
Beta strandi542 – 548Combined sources7
Beta strandi555 – 557Combined sources3
Helixi565 – 585Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QO8X-ray2.15A/D23-588[»]
ProteinModelPortaliQ9Z4P0.
SMRiQ9Z4P0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z4P0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 134Cytochrome cAdd BLAST111

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni135 – 588Flavoprotein-likeAdd BLAST454

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.
OMAiLMRKTTV.
OrthoDBiPOG091H02TE.

Family and domain databases

Gene3Di3.50.50.60. 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.
[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.

Q9Z4P0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLKYLVSAM ALVVLSSGTA MAKTPDMGSF HADMGSCQSC HAKPIKVTDS
60 70 80 90 100
ETHENAQCKS CHGEYAELAN DKLQFDPHNS HLGDINCTSC HKGHEEPKFY
110 120 130 140 150
CNECHSFDIK PMPFSDAKKK KSWDDGWDQD KIQKAIAAGP SETTQVLVVG
160 170 180 190 200
AGSAGFNASL AAKKAGANVI LVDKAPFSGG NSMISAGGMN AVGTKQQTAH
210 220 230 240 250
GVEDKVEWFI EDAMKGGRQQ NDIKLVTILA EQSADGVQWL ESLGANLDDL
260 270 280 290 300
KRSGGARVDR THRPHGGKSS GPEIIDTLRK AAKEQGIDTR LNSRVVKLVV
310 320 330 340 350
NDDHSVVGAV VHGKHTGYYM IGAKSVVLAT GGYGMNKEMI AYYRPTMKDM
360 370 380 390 400
TSSNNITATG DGVLMAKEIG ASMTDIDWVQ AHPTVGKDSR ILISETVRGV
410 420 430 440 450
GAVMVNKDGN RFISELTTRD KASDAILKQP GQFAWIIFDN QLYKKAKMVR
460 470 480 490 500
GYDHLEMLYK GDTVEQLAKS TGMKVADLAK TVSDYNGYVA SGKDTAFGRA
510 520 530 540 550
DMPLNMTQSP YYAVKVAPGI HHTMGGVAIN TTASVLDLQS KPIDGLFAAG
560 570 580
EVTGGVHGYN RLGGNAIADT VVFGRIAGDN AAKHALDK
Length:588
Mass (Da):62,946
Last modified:May 1, 1999 - v1
Checksum:i99C4AE25814693D2
GO

Mass spectrometryi

Molecular mass is 63985±0.1 Da from positions 23 - 588. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ236923 Genomic DNA. Translation: CAB37062.1.
CP000447 Genomic DNA. Translation: ABI72427.1.
RefSeqiWP_011638036.1. NC_008345.1.

Genome annotation databases

EnsemblBacteriaiABI72427; ABI72427; Sfri_2586.
KEGGisfr:Sfri_2586.
PATRICi23499229. VBISheFri14343_2684.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ236923 Genomic DNA. Translation: CAB37062.1.
CP000447 Genomic DNA. Translation: ABI72427.1.
RefSeqiWP_011638036.1. NC_008345.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QO8X-ray2.15A/D23-588[»]
ProteinModelPortaliQ9Z4P0.
SMRiQ9Z4P0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318167.Sfri_2586.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PRIDEiQ9Z4P0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI72427; ABI72427; Sfri_2586.
KEGGisfr:Sfri_2586.
PATRICi23499229. VBISheFri14343_2684.

Phylogenomic databases

eggNOGiENOG4107EFR. Bacteria.
COG1053. LUCA.
HOGENOMiHOG000227327.
KOiK00244.
OMAiLMRKTTV.
OrthoDBiPOG091H02TE.

Miscellaneous databases

EvolutionaryTraceiQ9Z4P0.

Family and domain databases

Gene3Di3.50.50.60. 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.
[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 nameiFRD2_SHEFN
AccessioniPrimary (citable) accession number: Q9Z4P0
Secondary accession number(s): Q07ZY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.