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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311Iron (heme 2 axial ligand)
Binding sitei37 – 371Heme 1 (covalent)
Binding sitei40 – 401Heme 1 (covalent)
Metal bindingi41 – 411Iron (heme 1 axial ligand)
Binding sitei58 – 581Heme 2 (covalent)
Binding sitei61 – 611Heme 2 (covalent)
Metal bindingi62 – 621Iron (heme 2 axial ligand)
Metal bindingi78 – 781Iron (heme 3 axial ligand)
Metal bindingi81 – 811Iron (heme 4 axial ligand)
Binding sitei87 – 871Heme 3 (covalent)
Binding sitei90 – 901Heme 3 (covalent)
Metal bindingi91 – 911Iron (heme 3 axial ligand)
Metal bindingi94 – 941Iron (heme 1 axial ligand)
Binding sitei101 – 1011Heme 4 (covalent)
Binding sitei104 – 1041Heme 4 (covalent)
Metal bindingi105 – 1051Iron (heme 4 axial ligand)
Active sitei382 – 3821By similarity
Active sitei398 – 3981By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi146 – 16015FADSequence analysisAdd
BLAST

GO - Molecular functioni

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

BioCyciSFRI318167:GIXS-2670-MONOMER.

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

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 588566Fumarate reductase flavoprotein subunitPRO_0000010346Add
BLAST

Expressioni

Inductioni

By anaerobic growth on Fe3+ ions.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi318167.Sfri_2586.

Structurei

Secondary structure

1
588
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 348Combined sources
Helixi37 – 393Combined sources
Helixi52 – 6211Combined sources
Helixi65 – 684Combined sources
Beta strandi71 – 755Combined sources
Helixi87 – 893Combined sources
Beta strandi93 – 953Combined sources
Helixi100 – 1034Combined sources
Turni113 – 1164Combined sources
Helixi129 – 1379Combined sources
Beta strandi141 – 1499Combined sources
Helixi153 – 16513Combined sources
Beta strandi169 – 1724Combined sources
Beta strandi174 – 1785Combined sources
Helixi182 – 1843Combined sources
Helixi195 – 1995Combined sources
Helixi206 – 21611Combined sources
Turni217 – 2193Combined sources
Helixi223 – 24220Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi265 – 2684Combined sources
Helixi270 – 28415Combined sources
Beta strandi292 – 3009Combined sources
Beta strandi304 – 31310Combined sources
Turni314 – 3163Combined sources
Beta strandi317 – 32812Combined sources
Helixi337 – 3437Combined sources
Helixi345 – 3473Combined sources
Helixi361 – 3688Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi379 – 38911Combined sources
Helixi396 – 3994Combined sources
Beta strandi403 – 4053Combined sources
Helixi419 – 4279Combined sources
Helixi430 – 4323Combined sources
Beta strandi434 – 4396Combined sources
Helixi440 – 4456Combined sources
Helixi447 – 4548Combined sources
Beta strandi459 – 4635Combined sources
Helixi464 – 4707Combined sources
Helixi475 – 49117Combined sources
Turni495 – 4973Combined sources
Beta strandi508 – 52316Combined sources
Beta strandi534 – 5374Combined sources
Beta strandi542 – 5487Combined sources
Beta strandi555 – 5573Combined sources
Helixi565 – 58521Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO8X-ray2.15A/D23-588[»]
ProteinModelPortaliQ9Z4P0.
SMRiQ9Z4P0. Positions 24-587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z4P0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 134111Cytochrome cAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 588454Flavoprotein-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

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO8X-ray2.15A/D23-588[»]
ProteinModelPortaliQ9Z4P0.
SMRiQ9Z4P0. Positions 24-587.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318167.Sfri_2586.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

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.

Enzyme and pathway databases

BioCyciSFRI318167:GIXS-2670-MONOMER.

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: September 7, 2016
This is version 126 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.