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Protein

Fumarate reductase flavoprotein subunit

Gene

fccA

Organism
Shewanella frigidimarina
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.

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8Iron (heme 2 axial ligand)1
Binding sitei14Heme 1 (covalent)1
Binding sitei17Heme 1 (covalent)1
Metal bindingi18Iron (heme 1 axial ligand)1
Binding sitei36Heme 2 (covalent)1
Binding sitei39Heme 2 (covalent)1
Metal bindingi40Iron (heme 2 axial ligand)1
Metal bindingi58Iron (heme 3 axial ligand)1
Metal bindingi61Iron (heme 4 axial ligand)1
Binding sitei68Heme 3 (covalent)1
Binding sitei71Heme 3 (covalent)1
Metal bindingi72Iron (heme 3 axial ligand)1
Metal bindingi75Iron (heme 1 axial ligand)1
Binding sitei82Heme 4 (covalent)1
Binding sitei85Heme 4 (covalent)1
Metal bindingi86Iron (heme 4 axial ligand)1
Binding sitei365Substrate1
Binding sitei377Substrate1
Active sitei402Proton donor1
Binding sitei504Substrate1
Binding sitei544Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi132 – 143FAD1 PublicationAdd BLAST12
Nucleotide bindingi156 – 157FAD1 Publication2
Nucleotide bindingi164 – 165FAD1 Publication2
Nucleotide bindingi169 – 171FAD1 Publication3
Nucleotide bindingi549 – 550FAD1 Publication2

GO - Molecular functioni

  • electron carrier activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • succinate dehydrogenase activity Source: InterPro

GO - Biological processi

  • anaerobic electron transport chain Source: UniProtKB
  • anaerobic respiration Source: UniProtKB
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

SABIO-RKP0C278.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate reductase flavoprotein subunit (EC:1.3.5.4)
Alternative name(s):
Flavocytochrome c
Flavocytochrome c3
Short name:
Fcc3
Gene namesi
Name:fccA
Synonyms:fcc3
OrganismiShewanella frigidimarina
Taxonomic identifieri56812 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi61H → A: Reduces catalytic activity 10-fold. Reduces affinity for fumarate. 1 Publication1
Mutagenesisi61H → M: Reduces catalytic activity 5-fold. Reduces affinity for fumarate. 1 Publication1
Mutagenesisi365H → A: Reduces catalytic activity by over 75%. 1 Publication1
Mutagenesisi378E → D: Strongly reduced affinity for substrate. Reduces activity 10000-fold. 1 Publication1
Mutagenesisi381R → M: Strongly reduced catalytic activity. No effect on substrate affinity. 1 Publication1
Mutagenesisi402R → A: Loss of activity. 2 Publications1
Mutagenesisi402R → K or Y: Reduces activity 10000-fold. 2 Publications1
Mutagenesisi504H → A: Reduces catalytic activity by over 64%. 1 Publication1

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000103441 – 571Fumarate reductase flavoprotein subunitAdd BLAST571

Expressioni

Inductioni

By anaerobiosis and fumarate.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi318167.Sfri_3690.

Structurei

Secondary structure

1571
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 9Combined sources6
Helixi14 – 16Combined sources3
Helixi30 – 40Combined sources11
Helixi43 – 47Combined sources5
Turni57 – 59Combined sources3
Helixi68 – 70Combined sources3
Beta strandi74 – 76Combined sources3
Helixi81 – 84Combined sources4
Helixi107 – 111Combined sources5
Helixi112 – 120Combined sources9
Beta strandi124 – 126Combined sources3
Beta strandi128 – 132Combined sources5
Helixi136 – 147Combined sources12
Beta strandi152 – 155Combined sources4
Beta strandi157 – 161Combined sources5
Helixi165 – 167Combined sources3
Helixi178 – 182Combined sources5
Helixi189 – 199Combined sources11
Turni200 – 202Combined sources3
Helixi206 – 225Combined sources20
Beta strandi232 – 234Combined sources3
Beta strandi244 – 247Combined sources4
Turni248 – 250Combined sources3
Helixi253 – 267Combined sources15
Beta strandi271 – 283Combined sources13
Beta strandi289 – 296Combined sources8
Turni297 – 299Combined sources3
Beta strandi300 – 305Combined sources6
Beta strandi307 – 311Combined sources5
Helixi320 – 326Combined sources7
Helixi328 – 330Combined sources3
Beta strandi335 – 337Combined sources3
Helixi344 – 351Combined sources8
Beta strandi356 – 358Combined sources3
Beta strandi362 – 369Combined sources8
Turni370 – 372Combined sources3
Beta strandi373 – 375Combined sources3
Helixi379 – 382Combined sources4
Beta strandi386 – 388Combined sources3
Helixi402 – 410Combined sources9
Helixi413 – 415Combined sources3
Beta strandi417 – 422Combined sources6
Helixi423 – 428Combined sources6
Helixi432 – 438Combined sources7
Beta strandi443 – 446Combined sources4
Helixi447 – 454Combined sources8
Helixi458 – 474Combined sources17
Turni478 – 480Combined sources3
Beta strandi494 – 506Combined sources13
Beta strandi509 – 512Combined sources4
Beta strandi517 – 519Combined sources3
Beta strandi525 – 531Combined sources7
Beta strandi536 – 540Combined sources5
Helixi548 – 567Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E39X-ray1.80A1-571[»]
1JRXX-ray2.00A/B1-571[»]
1JRYX-ray2.00A/B1-571[»]
1JRZX-ray2.00A/B1-571[»]
1KSSX-ray1.80A1-571[»]
1KSUX-ray2.00A/B1-571[»]
1LJ1X-ray2.00A/B1-571[»]
1M64X-ray1.80A/B1-571[»]
1P2EX-ray2.20A1-571[»]
1P2HX-ray2.10A1-571[»]
1Q9IX-ray1.60A1-571[»]
1QJDX-ray1.80A1-571[»]
1Y0PX-ray1.50A1-571[»]
2B7RX-ray1.70A1-571[»]
2B7SX-ray2.12A1-571[»]
ProteinModelPortaliP0C278.
SMRiP0C278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C278.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 117Cytochrome cAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni118 – 571Flavoprotein-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

Phylogenomic databases

eggNOGiCOG1053. LUCA.

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.
IPR007087. Znf_C2H2.
[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.

P0C278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADNLAEFHVQ NQECDSCHTP DGELSNDSLT YENTQCVSCH GTLEEVAETT
60 70 80 90 100
KHEHYNAHAS HFPGEVACTS CHSAHEKSMV YCDSCHSFDF NMPYAKKWQR
110 120 130 140 150
DEPTIAELAK DKSERQAALA SAPHDTVDVV VVGSGGAGFS AAISATDSGA
160 170 180 190 200
KVILIEKEPV IGGNAKLAAG GMNAAWTDQQ KAKKITDSPE LMFEDTMKGG
210 220 230 240 250
QNINDPALVK VLSSHSKDSV DWMTAMGADL TDVGMMGGAS VNRAHRPTGG
260 270 280 290 300
AGVGAHVVQV LYDNAVKRNI DLRMNTRGIE VLKDDKGTVK GILVKGMYKG
310 320 330 340 350
YYWVKADAVI LATGGFAKNN ERVAKLDPSL KGFISTNQPG AVGDGLDVAE
360 370 380 390 400
NAGGALKDMQ YIQAHPTLSV KGGVMVTEAV RGNGAILVNR EGKRFVNEIT
410 420 430 440 450
TRDKASAAIL AQTGKSAYLI FDDSVRKSLS KIDKYIGLGV APTADSLVKL
460 470 480 490 500
GKMEGIDGKA LTETVARYNS LVSSGKDTDF ERPNLPRALN EGNYYAIEVT
510 520 530 540 550
PGVHHTMGGV MIDTKAEVMN AKKQVIPGLY GAGEVTGGVH GANRLGGNAI
560 570
SDIITFGRLA GEEAAKYSKK N
Length:571
Mass (Da):60,621
Last modified:December 12, 2006 - v1
Checksum:iD2E4FC43C9A6484C
GO

Mass spectrometryi

Molecular mass is 63033±10 Da from positions 1 - 571. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132010 Genomic DNA. Translation: CAB38558.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132010 Genomic DNA. Translation: CAB38558.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E39X-ray1.80A1-571[»]
1JRXX-ray2.00A/B1-571[»]
1JRYX-ray2.00A/B1-571[»]
1JRZX-ray2.00A/B1-571[»]
1KSSX-ray1.80A1-571[»]
1KSUX-ray2.00A/B1-571[»]
1LJ1X-ray2.00A/B1-571[»]
1M64X-ray1.80A/B1-571[»]
1P2EX-ray2.20A1-571[»]
1P2HX-ray2.10A1-571[»]
1Q9IX-ray1.60A1-571[»]
1QJDX-ray1.80A1-571[»]
1Y0PX-ray1.50A1-571[»]
2B7RX-ray1.70A1-571[»]
2B7SX-ray2.12A1-571[»]
ProteinModelPortaliP0C278.
SMRiP0C278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318167.Sfri_3690.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1053. LUCA.

Enzyme and pathway databases

SABIO-RKP0C278.

Miscellaneous databases

EvolutionaryTraceiP0C278.

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.
IPR007087. Znf_C2H2.
[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_SHEFR
AccessioniPrimary (citable) accession number: P0C278
Secondary accession number(s): Q02469, Q9X969
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: November 2, 2016
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The N-terminal sequence has been extracted from PDB entry 1LJ1.Curated

Keywords - Technical termi

3D-structure

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.