Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0C278

- FRDA_SHEFR

UniProt

P0C278 - FRDA_SHEFR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fumarate reductase flavoprotein subunit

Gene

fccA

Organism
Shewanella frigidimarina
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.

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Iron (heme 2 axial ligand)
Binding sitei14 – 141Heme 1 (covalent)
Binding sitei17 – 171Heme 1 (covalent)
Metal bindingi18 – 181Iron (heme 1 axial ligand)
Binding sitei36 – 361Heme 2 (covalent)
Binding sitei39 – 391Heme 2 (covalent)
Metal bindingi40 – 401Iron (heme 2 axial ligand)
Metal bindingi58 – 581Iron (heme 3 axial ligand)
Metal bindingi61 – 611Iron (heme 4 axial ligand)
Binding sitei68 – 681Heme 3 (covalent)
Binding sitei71 – 711Heme 3 (covalent)
Metal bindingi72 – 721Iron (heme 3 axial ligand)
Metal bindingi75 – 751Iron (heme 1 axial ligand)
Binding sitei82 – 821Heme 4 (covalent)
Binding sitei85 – 851Heme 4 (covalent)
Metal bindingi86 – 861Iron (heme 4 axial ligand)
Binding sitei365 – 3651Substrate
Binding sitei377 – 3771Substrate
Active sitei402 – 4021Proton donor
Binding sitei504 – 5041Substrate
Binding sitei544 – 5441Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi132 – 14312FAD1 PublicationAdd
BLAST
Nucleotide bindingi156 – 1572FAD1 Publication
Nucleotide bindingi164 – 1652FAD1 Publication
Nucleotide bindingi169 – 1713FAD1 Publication
Nucleotide bindingi549 – 5502FAD1 Publication

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. succinate dehydrogenase activity Source: InterPro

GO - Biological processi

  1. anaerobic electron transport chain Source: UniProtKB
  2. 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

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

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611H → A: Reduces catalytic activity 10-fold. Reduces affinity for fumarate. 1 Publication
Mutagenesisi61 – 611H → M: Reduces catalytic activity 5-fold. Reduces affinity for fumarate. 1 Publication
Mutagenesisi365 – 3651H → A: Reduces catalytic activity by over 75%. 1 Publication
Mutagenesisi378 – 3781E → D: Strongly reduced affinity for substrate. Reduces activity 10000-fold. 1 Publication
Mutagenesisi381 – 3811R → M: Strongly reduced catalytic activity. No effect on substrate affinity. 1 Publication
Mutagenesisi402 – 4021R → A: Loss of activity. 2 Publications
Mutagenesisi402 – 4021R → K or Y: Reduces activity 10000-fold. 2 Publications
Mutagenesisi504 – 5041H → A: Reduces catalytic activity by over 64%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571Fumarate reductase flavoprotein subunitPRO_0000010344Add
BLAST

Expressioni

Inductioni

By anaerobiosis and fumarate.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
571
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96Combined sources
Helixi14 – 163Combined sources
Helixi30 – 4011Combined sources
Helixi43 – 475Combined sources
Turni57 – 593Combined sources
Helixi68 – 703Combined sources
Beta strandi74 – 763Combined sources
Helixi81 – 844Combined sources
Helixi107 – 1115Combined sources
Helixi112 – 1209Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1325Combined sources
Helixi136 – 14712Combined sources
Beta strandi152 – 1554Combined sources
Beta strandi157 – 1615Combined sources
Helixi165 – 1673Combined sources
Helixi178 – 1825Combined sources
Helixi189 – 19911Combined sources
Turni200 – 2023Combined sources
Helixi206 – 22520Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi244 – 2474Combined sources
Turni248 – 2503Combined sources
Helixi253 – 26715Combined sources
Beta strandi271 – 28313Combined sources
Beta strandi289 – 2968Combined sources
Turni297 – 2993Combined sources
Beta strandi300 – 3056Combined sources
Beta strandi307 – 3115Combined sources
Helixi320 – 3267Combined sources
Helixi328 – 3303Combined sources
Beta strandi335 – 3373Combined sources
Helixi344 – 3518Combined sources
Beta strandi356 – 3583Combined sources
Beta strandi362 – 3698Combined sources
Turni370 – 3723Combined sources
Beta strandi373 – 3753Combined sources
Helixi379 – 3824Combined sources
Beta strandi386 – 3883Combined sources
Helixi402 – 4109Combined sources
Helixi413 – 4153Combined sources
Beta strandi417 – 4226Combined sources
Helixi423 – 4286Combined sources
Helixi432 – 4387Combined sources
Beta strandi443 – 4464Combined sources
Helixi447 – 4548Combined sources
Helixi458 – 47417Combined sources
Turni478 – 4803Combined sources
Beta strandi494 – 50613Combined sources
Beta strandi509 – 5124Combined sources
Beta strandi517 – 5193Combined sources
Beta strandi525 – 5317Combined sources
Beta strandi536 – 5405Combined sources
Helixi548 – 56720Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-568.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C278.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 117117Cytochrome cAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni118 – 571454Flavoprotein-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

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.
IPR007087. Znf_C2H2.
[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.

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
Entry Method Resolution (Å) Chain Positions PDBsum
1E39 X-ray 1.80 A 1-571 [» ]
1JRX X-ray 2.00 A/B 1-571 [» ]
1JRY X-ray 2.00 A/B 1-571 [» ]
1JRZ X-ray 2.00 A/B 1-571 [» ]
1KSS X-ray 1.80 A 1-571 [» ]
1KSU X-ray 2.00 A/B 1-571 [» ]
1LJ1 X-ray 2.00 A/B 1-571 [» ]
1M64 X-ray 1.80 A/B 1-571 [» ]
1P2E X-ray 2.20 A 1-571 [» ]
1P2H X-ray 2.10 A 1-571 [» ]
1Q9I X-ray 1.60 A 1-571 [» ]
1QJD X-ray 1.80 A 1-571 [» ]
1Y0P X-ray 1.50 A 1-571 [» ]
2B7R X-ray 1.70 A 1-571 [» ]
2B7S X-ray 2.12 A 1-571 [» ]
ProteinModelPortali P0C278.
SMRi P0C278. Positions 1-568.
ModBasei Search...
MobiDBi Search...

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P0C278.

Miscellaneous databases

EvolutionaryTracei P0C278.

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.
IPR007087. Znf_C2H2.
[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

  1. "Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina."
    Pealing S.L., Lysek D.A., Taylor P., Alexeev D., Reid G.A., Chapman S.K., Walkinshaw M.D.
    J. Struct. Biol. 127:76-78(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-571, CRYSTALLIZATION.
    Strain: ACAM591.
  2. "Structural and mechanistic mapping of a unique fumarate reductase."
    Taylor P., Pealing S.L., Reid G.A., Chapman S.K., Walkinshaw M.D.
    Nat. Struct. Biol. 6:1108-1112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  3. "Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study."
    Doherty M.K., Pealing S.L., Miles C.S., Moysey R., Taylor P., Walkinshaw M.D., Reid G.A., Chapman S.K.
    Biochemistry 39:10695-10701(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-365 AND ALA-504 IN COMPLEX WITH FAD; FUMARATE AND HEMES, MUTAGENESIS OF HIS-365; ARG-402 AND HIS-504.
  4. "Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase."
    Mowat C.G., Moysey R., Miles C.S., Leys D., Doherty M.K., Taylor P., Walkinshaw M.D., Reid G.A., Chapman S.K.
    Biochemistry 40:12292-12298(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-402; LYS-402 AND TYR-402, MUTAGENESIS OF ARG-402, ENZYME KINETICS.
  5. "Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina."
    Pankhurst K.L., Mowat C.G., Miles C.S., Leys D., Walkinshaw M.D., Reid G.A., Chapman S.K.
    Biochemistry 41:8551-8556(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-505 AND TYR-505, CHARACTERIZATION.
  6. "Engineering water to act as an active site acid catalyst in a soluble fumarate reductase."
    Mowat C.G., Pankhurst K.L., Miles C.S., Leys D., Walkinshaw M.D., Reid G.A., Chapman S.K.
    Biochemistry 41:11990-11996(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS PHE-363 AND PHE-363/ALA-402, CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina."
    Rothery E.L., Mowat C.G., Miles C.S., Walkinshaw M.D., Reid G.A., Chapman S.K.
    Biochemistry 42:13160-13169(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ALA-61 AND MET-61 IN COMPLEXES WITH HEME; SUBSTRATE AND FAD, MASS SPECTROMETRY, MUTAGENESIS OF HIS-61.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANT CYS-251/CYS430.
  9. "A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina."
    Pankhurst K.L., Mowat C.G., Rothery E.L., Hudson J.M., Jones A.K., Miles C.S., Walkinshaw M.D., Armstrong F.A., Reid G.A., Chapman S.K.
    J. Biol. Chem. 281:20589-20597(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ASP-378 AND MET-381, MUTAGENESIS OF GLU-378 AND ARG-381, IDENTIFICATION BY MASS SPECTROMETRY.

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 26, 2014
This is version 41 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

External Data

Dasty 3