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Protein

Photosynthetic reaction center cytochrome c subunit

Gene

pufC

Organism
Thermochromatium tepidum (Chromatium tepidum)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi94Iron (heme 1 axial ligand)UniRule annotationCombined sources1 Publication1
Binding sitei107Heme 1 (covalent)UniRule annotationCombined sources1 Publication1
Binding sitei110Heme 1 (covalent)UniRule annotationCombined sources1 Publication1
Metal bindingi111Iron (heme 1 axial ligand); via tele nitrogenUniRule annotationCombined sources1 Publication1
Metal bindingi130Iron (heme 2 axial ligand)UniRule annotationCombined sources1 Publication1
Metal bindingi144Iron (heme 4 axial ligand); via tele nitrogenUniRule annotationCombined sources1 Publication1
Binding sitei152Heme 2 (covalent)UniRule annotationCombined sources1 Publication1
Binding sitei155Heme 2 (covalent)UniRule annotationCombined sources1 Publication1
Metal bindingi156Iron (heme 2 axial ligand); via tele nitrogenUniRule annotationCombined sources1 Publication1
Metal bindingi236Iron (heme 3 axial ligand)UniRule annotationCombined sources1 Publication1
Binding sitei247Heme 3 (covalent)UniRule annotationCombined sources1 Publication1
Binding sitei250Heme 3 (covalent)UniRule annotationCombined sources1 Publication1
Metal bindingi251Iron (heme 3 axial ligand); via tele nitrogenUniRule annotationCombined sources1 Publication1
Binding sitei307Heme 4 (covalent)UniRule annotationCombined sources1 Publication1
Binding sitei310Heme 4 (covalent)UniRule annotationCombined sources1 Publication1
Metal bindingi311Iron (heme 4 axial ligand); via tele nitrogenUniRule annotationCombined sources1 Publication1

GO - Molecular functioni

  • electron transfer activity Source: InterPro
  • heme binding Source: UniProtKB
  • iron ion binding Source: InterPro

GO - Biological processi

Keywordsi

Biological processElectron transport, Photosynthesis, Transport
LigandHeme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Photosynthetic reaction center cytochrome c subunit1 PublicationUniRule annotationImported
Gene namesi
Name:pufCImported
OrganismiThermochromatium tepidum (Chromatium tepidum)Imported
Taxonomic identifieri1050 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThermochromatium

Subcellular locationi

  • Cellular chromatophore membrane 1 Publication; Lipid-anchor 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Membrane, Reaction center

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000043712423 – 404Photosynthetic reaction center cytochrome c subunitAdd BLAST382

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi23N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi23S-diacylglycerol cysteinePROSITE-ProRule annotation1

Post-translational modificationi

Binds 4 heme groups per subunit.UniRule annotation1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Subunit structurei

Component of the photosynthetic reaction center composed of protein subunits L (PufL), M (PufM), H (PuhA) and cytochrome C (PufC). The reaction center interacts with light-harvesting antenna complex LH1.1 Publication

Protein-protein interaction databases

DIPiDIP-60696N
IntActiD2Z0P5, 1 interactor

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 32Combined sources4
Beta strandi41 – 44Combined sources4
Helixi46 – 55Combined sources10
Beta strandi69 – 71Combined sources3
Helixi72 – 75Combined sources4
Beta strandi76 – 78Combined sources3
Beta strandi80 – 82Combined sources3
Beta strandi84 – 86Combined sources3
Helixi87 – 101Combined sources15
Turni103 – 105Combined sources3
Helixi107 – 109Combined sources3
Beta strandi110 – 112Combined sources3
Beta strandi115 – 117Combined sources3
Helixi122 – 140Combined sources19
Helixi142 – 145Combined sources4
Turni146 – 148Combined sources3
Helixi152 – 156Combined sources5
Helixi188 – 190Combined sources3
Helixi200 – 203Combined sources4
Beta strandi215 – 221Combined sources7
Helixi226 – 243Combined sources18
Helixi247 – 249Combined sources3
Helixi253 – 255Combined sources3
Helixi259 – 261Combined sources3
Helixi264 – 282Combined sources19
Helixi285 – 287Combined sources3
Turni288 – 290Combined sources3
Helixi293 – 295Combined sources3
Helixi307 – 311Combined sources5
Beta strandi314 – 316Combined sources3
Helixi317 – 320Combined sources4
Helixi324 – 326Combined sources3
Helixi328 – 330Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WMMX-ray3.01C1-404[»]
4V8KX-ray3.01AC/BC1-404[»]
5B5MX-ray3.30C/o1-333[»]
5B5NX-ray3.30C/o1-333[»]
5Y5SX-ray1.90C1-404[»]
SMRiD2Z0P5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi339 – 401Ala-richPROSITE-ProRule annotationAdd BLAST63

Keywords - Domaini

Signal

Family and domain databases

CDDicd09224 CytoC_RC, 1 hit
Gene3Di1.10.468.10, 3 hits
InterProiView protein in InterPro
IPR011031 Multihaem_cyt
IPR023119 Multihaem_cyt_PRC_cyt_su-like
IPR036280 Multihaem_cyt_sf
IPR003158 Photosyn_RC_cyt_c-su
PfamiView protein in Pfam
PF02276 CytoC_RC, 1 hit
PIRSFiPIRSF000017 RC_cytochrome, 1 hit
SUPFAMiSSF48695 SSF48695, 1 hit
PROSITEiView protein in PROSITE
PS51008 MULTIHEME_CYTC, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

D2Z0P5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPAQQLTLP AVIVVASVML LGCEGPPPGT EQIGYRGVGM ENYYNKRQRA
60 70 80 90 100
LSIQANQPVE SLPAADSTGP KASEVYQNVQ VLKDLSVGEF TRTMVAVTTW
110 120 130 140 150
VSPKEGCNYC HVPGNWASDD IYTKVVSRRM FELVRAANSD WKAHVAETGV
160 170 180 190 200
TCYTCHRGNP VPKYAWVTDP GPKYPSGLKP TGQNYGSKTV AYASLPFDPL
210 220 230 240 250
TPFLDQANEI RITGNAALAG SNPASLKQAE WTFGLMMNIS DSLGVGCTFC
260 270 280 290 300
HNTRAFNDWT QSTPKRTTAW YAIRHVRDIN QNYIWPLNDV LPASRKGPYG
310 320 330 340 350
DPLRVSCMTC HQAVNKPLYG AQMAKDYPGL YKTAVTQEAL AGSAPASEAA
360 370 380 390 400
PAAATEAAPE APAQEVPAAE AVPAAAEPGA AEAAGSVEPA PVEEVAPAPA

AQRL
Length:404
Mass (Da):43,140
Last modified:March 23, 2010 - v1
Checksum:i8C60811DBFC1E27C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti308M → S in BAF80147 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB543090 Genomic DNA Translation: BAI67784.1
D85518 Genomic DNA Translation: BAF80147.2

Similar proteinsi

Entry informationi

Entry nameiCYCR_THETI
AccessioniPrimary (citable) accession number: D2Z0P5
Secondary accession number(s): A8ASG7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 7, 2016
Last sequence update: March 23, 2010
Last modified: June 20, 2018
This is version 33 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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