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Q6Y9H0 (RBL2_PROMN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase
Short name=RuBisCO
EC=4.1.1.39

Cleaved into the following 4 chains:

  1. Ribulose bisphosphate carboxylase 1
  2. Ribulose bisphosphate carboxylase 2
  3. Ribulose bisphosphate carboxylase 3
  4. Ribulose bisphosphate carboxylase 4
Gene names
Name:rbcL
OrganismProrocentrum minimum (Dinoflagellate)
Taxonomic identifier39449 [NCBI]
Taxonomic lineageEukaryota › Alveolata › Dinophyceae › Prorocentrales › Prorocentraceae › Prorocentrum

Protein attributes

Sequence length1563 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity.

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastid › chloroplast Probable. Note: In this organism the plastid is the result of a secondary endosymbiosis event, and thus is found within the endomembrane system, necessitating a complex targeting process.

Post-translational modification

In Western blots an approximately 220 kDa polyprotein and 2 smaller proteins of about 55 and 52 kDa are detected, suggesting the polyprotein may be cleaved at one end of the linker and then at the other end to give mature RuBisCO.

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity.

Synthesized as an approximately 220 kDa polyprotein, imported into chloroplasts and subsequently cleaved into 4 mature RuBisCO proteins. Only the 2 middle RuBisCO copies are complete in this entry. There are estimated to be at least 10 copies of this polyprotein gene.

This may be first cotranslationally imported into the ER up to a stop-transfer signal, so that the N-terminal region of the transit peptide is in the lumen of the ER while the rest of the protein remains in the cytoplasm. Maintaining this topology, proteins are directed to the Golgi and sorted into vesicles that will fuse with the outermost plastid membrane, exposing the transit peptide to the Toc/Tic apparatus, which draws the entire protein across the remaining membranes By similarity.

Sequence similarities

Belongs to the RuBisCO large chain family. Type II subfamily.

Caution

Note that unlike other eukaryotes, peridinin-containing dinoflagellates have a nuclear-encoded chloroplast-targeted form II RuBisCO.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 196›196Ribulose bisphosphate carboxylase 1 Probable
PRO_0000042971
Propeptide197 – 21721Linker Probable
PRO_0000042972
Chain218 – 702485Ribulose bisphosphate carboxylase 2 Probable
PRO_0000042973
Propeptide703 – 72321Linker Probable
PRO_0000042974
Chain724 – 1208485Ribulose bisphosphate carboxylase 3 Probable
PRO_0000042975
Propeptide1209 – 122921Linker Probable
PRO_0000042976
Chain1230 – ›1563›334Ribulose bisphosphate carboxylase 4 Probable
PRO_0000042977

Sites

Active site3831Proton acceptor By similarity
Active site5041Proton acceptor By similarity
Active site8891Proton acceptor By similarity
Active site10101Proton acceptor By similarity
Active site13951Proton acceptor By similarity
Active site15161Proton acceptor By similarity
Metal binding4081Magnesium; via carbamate group By similarity
Metal binding4101Magnesium By similarity
Metal binding4111Magnesium By similarity
Metal binding9141Magnesium; via carbamate group By similarity
Metal binding9161Magnesium By similarity
Metal binding9171Magnesium By similarity
Metal binding14201Magnesium; via carbamate group By similarity
Metal binding14221Magnesium By similarity
Metal binding14231Magnesium By similarity
Binding site321Substrate By similarity
Binding site791Substrate By similarity
Binding site3281Substrate; in homodimeric partner By similarity
Binding site3851Substrate By similarity
Binding site5051Substrate By similarity
Binding site5381Substrate By similarity
Binding site5851Substrate By similarity
Binding site8341Substrate; in homodimeric partner By similarity
Binding site8911Substrate By similarity
Binding site10111Substrate By similarity
Binding site10441Substrate By similarity
Binding site10911Substrate By similarity
Binding site13401Substrate; in homodimeric partner By similarity
Binding site13971Substrate By similarity
Binding site15171Substrate By similarity
Binding site15501Substrate By similarity
Site401Transition state stabilizer By similarity
Site5461Transition state stabilizer By similarity
Site10521Transition state stabilizer By similarity
Site15581Transition state stabilizer By similarity

Amino acid modifications

Modified residue4081N6-carboxylysine By similarity
Modified residue9141N6-carboxylysine By similarity
Modified residue14201N6-carboxylysine By similarity

Experimental info

Sequence conflict7021D → E in AAO13026. Ref.1
Sequence conflict712 – 7132TT → KA in AAO13026. Ref.1
Sequence conflict7201A → T in AAO13026. Ref.1
Sequence conflict12081D → E in AAO13026. Ref.1
Sequence conflict1218 – 12214TTRK → KART in AAO13026. Ref.1
Sequence conflict12261A → T in AAO13026. Ref.1
Non-terminal residue11
Non-terminal residue15631

Sequences

Sequence LengthMass (Da)Tools
Q6Y9H0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 071A3E54EF7D81AF

FASTA1,563169,955
        10         20         30         40         50         60 
GHGAVTSPQT QRGYTAFVHT KLSRVIGASG IHTGTMSFGK MEGDASDKNI GFMLQDDVAD 

        70         80         90        100        110        120 
GPYYRQEWEG MKQTTPIISG GMNALRLPAF FENLGHSNVI LTAGGGAFGH KDGPKQGAIS 

       130        140        150        160        170        180 
CAQGEESWKL WKAGTYGDVS LSDGVVEYAK THEELKGAFL TFQKDADQIY PGWKEKLGYT 

       190        200        210        220        230        240 
GESSVQAASF NWQKKDLAAA FVGASTTRKA SSVARRALDQ SSRYADLSLT EEDLIKNGQH 

       250        260        270        280        290        300 
VLVAYIMKPK AGYDYLATAA HFAAESSTGT NVNVCTTDDF TKTVDALVYY IDPENEEMKI 

       310        320        330        340        350        360 
AYPTALFDRN ITDGRAMMCS VLTLSIGNNQ GMGDVDYGKI YDIYFPPQYL RLFDGPSCCV 

       370        380        390        400        410        420 
IDMWRILGRG TVGGGLVVGT IIKPKLGLQP KPFGQACYGF WQGGDFIKND EPQGNQTFCQ 

       430        440        450        460        470        480 
MNECIPEVVK AMRAAQEETG QGKLFSANIT ADDPNEMIAR AKYILNQMGP MAENCAFLVD 

       490        500        510        520        530        540 
GYVAGGTAVT VARRNFPKQF LHYHRAGHGA VTSPQTQRGY TAFVHTKLSR VIGASGIHTG 

       550        560        570        580        590        600 
TMSFGKMEGD ASDKNIGFML QDDVADGPYY RQEWEGMKQT TPIISGGMNA LRLPAFFENL 

       610        620        630        640        650        660 
GHSNVILTAG GGAFGHKDGP KQGAISCAQG EESWKLWKAG TYGDVSLSDG VVEYAKTHEE 

       670        680        690        700        710        720 
LKGAFLTFQK DADQIYPGWK EKLGYTGESS VQAASFNWQK KDLAAAFVGA STTRKASSVA 

       730        740        750        760        770        780 
RRALDQSSRY ADLSLTEEDL IKNGQHVLVA YIMKPKAGYD YLATAAHFAA ESSTGTNVNV 

       790        800        810        820        830        840 
CTTDDFTKTV DALVYYIDPE NEEMKIAYPT ALFDRNITDG RAMMCSVLTL SIGNNQGMGD 

       850        860        870        880        890        900 
VDYGKIYDIY FPPQYLRLFD GPSCCVIDMW RILGRGTVGG GLVVGTIIKP KLGLQPKPFG 

       910        920        930        940        950        960 
QACYGFWQGG DFIKNDEPQG NQTFCQMNEC IPEVVKAMRA AQEETGQGKL FSANITADDP 

       970        980        990       1000       1010       1020 
NEMIARAKYI LNQMGPMAEN CAFLVDGYVA GGTAVTVARR NFPKQFLHYH RAGHGAVTSP 

      1030       1040       1050       1060       1070       1080 
QTQRGYTAFV HTKLSRVIGA SGIHTGTMSF GKMEGDASDK NIGFMLQDDV ADGPYYRQEW 

      1090       1100       1110       1120       1130       1140 
EGMKQTTPII SGGMNALRLP AFFENLGHSN VILTAGGGAF GHKDGPKQGA ISCAQGEESW 

      1150       1160       1170       1180       1190       1200 
KLWKAGTYGD VSLSDGVVEY AKTHEELKGA FLTFQKDADQ IYPGWKEKLG YTGESSVQAA 

      1210       1220       1230       1240       1250       1260 
SFNWQKKDLA AAFVGASTTR KASSVARRAL DQSSRYADLS LTEEDLIKNG QHVLVAYIMK 

      1270       1280       1290       1300       1310       1320 
PKAGYDYLAT AAHFAAESST GTNVNVCTTD DFTKTVDALV YYIDPENEEM KIAYPTALFD 

      1330       1340       1350       1360       1370       1380 
RNITDGRAMM CSVLTLSIGN NQGMGDVDYG KIYDIYFPPQ YLRLFDGPSC CVIDMWRILG 

      1390       1400       1410       1420       1430       1440 
RGTVGGGLVV GTIIKPKLGL QPKPFGQACY GFWQGGDFIK NDEPQGNQTF CQMNECIPEV 

      1450       1460       1470       1480       1490       1500 
VKAMRAAQEE TGQGKLFSAN ITADDPNEMI ARAKYILNQM GPMAENCAFL VDGYVAGGTA 

      1510       1520       1530       1540       1550       1560 
VTVARRNFPK QFLHYHRAGH GAVTSPQTQR GYTAFVHTKL SRVIGASGIH TGTMSFGKME 


GDA

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References

[1]"Complex gene structure of the form II Rubisco in the dinoflagellate Prorocentrum minimum (Dinophyceae)."
Zhang H., Lin S.
J. Phycol. 39:1160-1171(2003)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE COPY, DETECTION OF PROTEIN.
Strain: CCMP696.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY169179 mRNA. Translation: AAO13036.1.
AY169169 mRNA. Translation: AAO13026.1.

3D structure databases

ProteinModelPortalQ6Y9H0.
SMRQ6Y9H0. Positions 1-178, 1231-1563.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
Gene3DG3DSA:3.20.20.110. RuBisCO_large. 4 hits.
G3DSA:3.30.70.150. RuBisCO_large. 3 hits.
PfamPF00016. RuBisCO_large. 4 hits.
PF02788. RuBisCO_large_N. 3 hits.
[Graphical view]
SUPFAMSSF51649. RuBisCO_large. 4 hits.
SSF54966. RuBisCO_large. 3 hits.
PROSITEPS00157. RUBISCO_LARGE. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL2_PROMN
AccessionPrimary (citable) accession number: Q6Y9H0
Secondary accession number(s): Q6Y9I0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2004
Last modified: June 28, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents