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Protein

Phycoerythrocyanin beta chain

Gene

pccB

Organism
Mastigocladus laminosus (Fischerella sp.)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.

Absorptioni

Abs(max)=~550 nm

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Phycocyanobilin chromophore (covalent; via 1 link)
Binding sitei153 – 1531Phycocyanobilin chromophore (covalent; via 1 link)

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Bile pigment, Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
Phycoerythrocyanin beta chain
Gene namesi
Name:pccB
OrganismiMastigocladus laminosus (Fischerella sp.)
Taxonomic identifieri83541 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaStigonematalesMastigocladus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Phycobilisome, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Phycoerythrocyanin beta chainPRO_0000199171Add
BLAST

Post-translational modificationi

Contains two covalently linked bilin chromophores.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1310Combined sources
Turni14 – 163Combined sources
Helixi21 – 3212Combined sources
Helixi34 – 4613Combined sources
Helixi48 – 6215Combined sources
Helixi64 – 674Combined sources
Helixi76 – 9924Combined sources
Beta strandi100 – 1023Combined sources
Helixi103 – 1075Combined sources
Turni108 – 1125Combined sources
Helixi113 – 1208Combined sources
Helixi125 – 14218Combined sources
Helixi154 – 16815Combined sources
Turni169 – 1713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7JX-ray3.00B1-172[»]
2C7KX-ray3.20B1-172[»]
2C7LX-ray2.85B1-172[»]
ProteinModelPortaliP00313.
SMRiP00313. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00313.

Family & Domainsi

Sequence similaritiesi

Belongs to the phycobiliprotein family.Curated

Family and domain databases

Gene3Di1.10.490.20. 1 hit.
InterProiIPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.

Sequencei

Sequence statusi: Complete.

P00313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDAFSRVVE QADKKGAYLS NDEINALQAI VADSNKRLDV VNRLTSNASS
60 70 80 90 100
IVANAYRALV AERPQVFNPG GPCFHHRNQA ACIRDLGFIL RYVTYSVLAG
110 120 130 140 150
DTSVMDDRCL NGLRETYQAL GTPGDAVASG IKKMKEAALK IANDPNGITK
160 170
GDCSQLMSEL ASYFDRAAAA VA
Length:172
Mass (Da):18,487
Last modified:August 1, 1991 - v2
Checksum:i0247FCE313D0C27D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34254 Genomic DNA. Translation: AAC64653.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34254 Genomic DNA. Translation: AAC64653.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7JX-ray3.00B1-172[»]
2C7KX-ray3.20B1-172[»]
2C7LX-ray2.85B1-172[»]
ProteinModelPortaliP00313.
SMRiP00313. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00313.

Family and domain databases

Gene3Di1.10.490.20. 1 hit.
InterProiIPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genes encoding both subunits of phycoerythrocyanin, a light-harvesting biliprotein from the cyanobacterium Mastigocladus laminosus."
    Eberlein M., Kufer W.
    Gene 94:133-136(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete amino-acid sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus."
    Fueglistaller P., Suter F., Zuber H.
    Hoppe-Seyler's Z. Physiol. Chem. 364:691-712(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-171.
  3. "Chromopeptides from phycoerythrocyanin. Structure and linkage of the three bilin groups."
    Bishop J.E., Rapoport H., Klotz A.V., Chan C.F., Glazer A.N., Fueglistaller P., Zuber H.
    J. Am. Chem. Soc. 109:875-881(1987)
    Cited for: CHROMOPHORE STRUCTURE, CHROMOPHORE BINDING AT CYS-82 AND CYS-153.
  4. "Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A."
    Duerring M., Huber R., Bode W., Ruembelli R., Zuber H.
    J. Mol. Biol. 211:633-644(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  5. "Structural basis for the photochemistry of alpha-phycoerythrocyanin."
    Schmidt M., Patel A., Zhao Y., Reuter W.
    Biochemistry 46:416-423(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-162, CHROMOPHORE BINDING AT CYS-82.

Entry informationi

Entry nameiPHEB_MASLA
AccessioniPrimary (citable) accession number: P00313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: October 14, 2015
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.