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B8HLB1 (B8HLB1_CYAP4) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Photosystem I P700 chlorophyll a apoprotein A2 HAMAP-Rule MF_00482
EC=1.97.1.12 HAMAP-Rule MF_00482
Alternative name(s):
PsaB HAMAP-Rule MF_00482
Gene names
Name:psaB HAMAP-Rule MF_00482
Ordered Locus Names:Cyan7425_4670 EMBL ACL46976.1
OrganismCyanothece sp. (strain PCC 7425 / ATCC 29141) [Complete proteome] [HAMAP] EMBL ACL46976.1
Taxonomic identifier395961 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Cyanothece

Protein attributes

Sequence length742 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6 By similarity. HAMAP-Rule MF_00482

PsaA and psaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX By similarity. RuleBase RU003775

Catalytic activity

Reduced plastocyanin + oxidized ferredoxin + light = oxidized plastocyanin + reduced ferredoxin. HAMAP-Rule MF_00482

Cofactor

PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center By similarity. HAMAP-Rule MF_00482

Subunit structure

The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes By similarity. HAMAP-Rule MF_00482

Subcellular location

Cellular thylakoid membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00482.

Membrane; Multi-pass membrane protein By similarity RuleBase RU003775.

Sequence similarities

Belongs to the PsaA/PsaB family. RuleBase RU003775 HAMAP-Rule MF_00482

Ontologies

Keywords
   Biological processElectron transport RuleBase RU003775 HAMAP-Rule MF_00482
Photosynthesis
Transport
   Cellular componentMembrane
Photosystem I RuleBase RU003775 HAMAP-Rule MF_00482
Thylakoid HAMAP-Rule MF_00482
   DomainTransmembrane
Transmembrane helix HAMAP-Rule MF_00482
   Ligand4Fe-4S RuleBase RU003775 HAMAP-Rule MF_00482
Chlorophyll RuleBase RU003775 HAMAP-Rule MF_00482
Chromophore
Iron
Iron-sulfur
Magnesium RuleBase RU003775 HAMAP-Rule MF_00482
Metal-binding
   Molecular functionOxidoreductase HAMAP-Rule MF_00482
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

photosynthesis

Inferred from electronic annotation. Source: HAMAP

protein-chromophore linkage

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

photosystem I

Inferred from electronic annotation. Source: UniProtKB-KW

thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

chlorophyll binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Transmembrane39 – 7032Helical; Name=I By similarity HAMAP-Rule MF_00482
Transmembrane132 – 15625Helical; Name=II By similarity HAMAP-Rule MF_00482
Transmembrane173 – 19523Helical; Name=III By similarity HAMAP-Rule MF_00482
Transmembrane270 – 28718Helical; Name=IV By similarity HAMAP-Rule MF_00482
Transmembrane336 – 35924Helical; Name=V By similarity HAMAP-Rule MF_00482
Transmembrane370 – 40132Helical; Name=VI By similarity HAMAP-Rule MF_00482
Transmembrane421 – 45030Helical; Name=VII By similarity HAMAP-Rule MF_00482
Transmembrane522 – 54625Helical; Name=VIII By similarity HAMAP-Rule MF_00482
Transmembrane580 – 61132Helical; Name=IX By similarity HAMAP-Rule MF_00482
Transmembrane652 – 67322Helical; Name=X By similarity HAMAP-Rule MF_00482
Transmembrane710 – 73829Helical; Name=XI By similarity HAMAP-Rule MF_00482

Sites

Metal binding5671Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity HAMAP-Rule MF_00482
Metal binding5761Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity HAMAP-Rule MF_00482
Metal binding6621Magnesium (chlorophyll-a B1 axial ligand; P700 special pair) By similarity HAMAP-Rule MF_00482
Metal binding6701Magnesium (chlorophyll-a B3 axial ligand) By similarity HAMAP-Rule MF_00482
Binding site6781Chlorophyll-a B3 By similarity HAMAP-Rule MF_00482
Binding site6791Phylloquinone B By similarity HAMAP-Rule MF_00482

Sequences

Sequence LengthMass (Da)Tools
B8HLB1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 96B36B749D0A0B07

FASTA74282,907
        10         20         30         40         50         60 
MATRFPKFSQ DLAQDPTTRR IWYAIATAHD FESHDGMTEE NLYQKIFASH FGHLAIIFLW 

        70         80         90        100        110        120 
TSGSLFHVAW QGNFEQWIKD PLNIRPIAHA IWDPQFGKPA VDAFTQAGAS SPVDIAYSGV 

       130        140        150        160        170        180 
YHWWYTIGMR TNSDLYMGAI TLLLFAAVFL FAGWLHLQPK FRPSLAWFKN AESRLNHHLA 

       190        200        210        220        230        240 
GLFGVSSLAW AGHLIHVAIP EARGQHVGWD NFLSTMPHPA GLAPFFTGNW GVYAQNPDTA 

       250        260        270        280        290        300 
GHVFGTSEGA GTAILTFLGG FHPQTESLWL TDIAHHHLAI AVIFIIAGHM YRTNFGIGHS 

       310        320        330        340        350        360 
MKEIMNAHNP PQGTPFGGML GAGHQGMYDT YNNSLHFQLG WHLACLGVVT SLVAQHMYSL 

       370        380        390        400        410        420 
PPYAFIAQDH TTMAALYTHH QYIAGFLMVG AFAHGAIFLV RDYDPAANKN NVLARVLEHK 

       430        440        450        460        470        480 
EAIISHLSWV SLFLGFHTLG LYVHNDVVVA FGTPEKQILI EPVFAQFIQA AHGKVLYGFD 

       490        500        510        520        530        540 
TLLSNPDSIA TTAWPNYGNV WLPGWLDAIN SGTNSLFLTI GPGDFLVHHA IALGLHTTTL 

       550        560        570        580        590        600 
ILVKGALDAR GSKLMPDKKD FGYAFPCDGP GRGGTCDISG WDAFYLSMFW MLNTIGWVTF 

       610        620        630        640        650        660 
YWHWKHLGIW EGNVAQFNES STYLMGWLRD YLWLYSGPLI NGYNPFGMNN LAVWSWMFLF 

       670        680        690        700        710        720 
GHLVWATGFM FLISWRGYWQ ELIETLVWAH ERTPLANLVR WKDKPVALSI VQARLVGLAH 

       730        740 
FTVGYIVTYA AFLIASTAAK YG

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References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7425 / ATCC 29141.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001344 Genomic DNA. Translation: ACL46976.1.
RefSeqYP_002485337.1. NC_011884.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING395961.Cyan7425_4670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL46976; ACL46976; Cyan7425_4670.
GeneID7290623.
KEGGcyn:Cyan7425_4670.
PATRIC21570339. VBICyaSp30657_4659.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG04867.
HOGENOMHOG000276868.
KOK02690.
OMAAQFNESS.
ProtClustDBPRK13199.

Enzyme and pathway databases

BioCycCSP395961:GJDE-4516-MONOMER.

Family and domain databases

Gene3D1.20.1130.10. 1 hit.
HAMAPMF_00482. PSI_PsaB.
InterProIPR001280. PSI_PsaA/B.
IPR020586. PSI_PsaA/B_CS.
IPR006244. PSI_PsaB.
[Graphical view]
PfamPF00223. PsaA_PsaB. 1 hit.
[Graphical view]
PIRSFPIRSF002905. PSI_A. 1 hit.
PRINTSPR00257. PHOTSYSPSAAB.
TIGRFAMsTIGR01336. psaB. 1 hit.
PROSITEPS00419. PHOTOSYSTEM_I_PSAAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB8HLB1_CYAP4
AccessionPrimary (citable) accession number: B8HLB1
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info