Reviewed, UniProtKB/Swiss-Prot Q5ENN5 (RBL2_HETTR)

Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase, chloroplastic
      Short name=RuBisCO
    EC=4.1.1.39

Gene names

Name:

rbcL

Organism

Heterocapsa triquetra (Dinoflagellate)

Taxonomic identifier

66468 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Dinophyceae › Peridiniales › Heterocapsaceae › Heterocapsa

Protein attributes

Sequence length	740 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 membrane 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.
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. This protein is suggested in Ref.1 to be first co-translationally imported into the ER up to the 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.
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.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photorespiration Photosynthesis
Cellular component	Chloroplast Membrane Plastid
Domain	Signal Transit peptide Transmembrane
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW photorespiration Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Transit peptide	23 – 55	33	Chloroplast Potential
	Chain	56 – 740	685	Ribulose bisphosphate carboxylase, chloroplastic		PRO_0000042970
Regions
	Transmembrane	56 – 76	21	Stop-transfer Potential
Sites
	Active site	268	1	Proton acceptor By similarity
	Active site	389	1	Proton acceptor By similarity
	Metal binding	293	1	Magnesium; via carbamate group By similarity
	Metal binding	295	1	Magnesium By similarity
	Metal binding	296	1	Magnesium By similarity
	Binding site	213	1	Substrate; in homodimeric partner By similarity
	Binding site	270	1	Substrate By similarity
	Binding site	390	1	Substrate By similarity
	Binding site	423	1	Substrate By similarity
	Binding site	470	1	Substrate By similarity
	Site	431	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	293	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5ENN5-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: E13467039029BA77	FASTA	740	79,148
	10 20 30 40 50 60 MPSSSFTTGL ALGAGALVGA NAFVAPTAKT TNLRAPTQEA SLQVAASQQT EQPAPSTSAL 70 80 90 100 110 120 PWAFGAGACL ALAAGGQRKQ RSAIAQGRAT VLPTASPVVR RALDQSSRYA DLSLSEEQLI 130 140 150 160 170 180 ANGKHVLVSY IMKPKAGYDY LATAAHFAAE SSTGTNVNVC TTDDFTKSVD ALVYYIDPEN 190 200 210 220 230 240 EECKIAYPNL LFDRNIIDGR AMMCSVLTLT IGNNQGMGDV EYGKIYDIYF PPSYLRLFDG 250 260 270 280 290 300 PSCNIIDMWR ILGRGTTDGG LVVGTIIKPK LGLQPKPFGE ACYAFWQGGD FIKNDEPQGN 310 320 330 340 350 360 QPFCQMNEVI PEVVKAMRAA IKETGVAKLF SANITADDPA EMIARGKYVL AQFGPLSENC 370 380 390 400 410 420 AFLVDGYVAG GTAVTVARRN FPKQFLHYHR AGHGSVTSPQ TQRGYTAFVH TKLSRVQGAS 430 440 450 460 470 480 GIHVGTMSFG KMEGDASDKN IAFMLQDDAA DGPYYHQTWE GMAETTPIIS GGMNALRLPA 490 500 510 520 530 540 FFENLGHSNV ILTAGGGAFG HKDGPKQGAT SCRQGEEAWK LWKAGVYGSV SLSDGVIEYA 550 560 570 580 590 600 KTHEEIKGAF LTFQKDADQI YPGWKEKLGY TGESSVQAAS FDWKKKAAAA AFAGSSTQAR 610 620 630 640 650 660 TVGVQMRHGY DDVATNTFYY DKRLESFGQQ EFFNQVGYLP DGTPMNTAGN LTNHPETIGP 670 680 690 700 710 720 DPHINGSELP QAVFVNSIGY LPDGTAMNQA GNAVNHPETM GPDLHMAGSP LPPPLKGYLN 730 740 DIGYLSDGTP MATAGNLSNH

References

[1]	"Complex protein targeting to dinoflagellate plastids." Patron N.J., Waller R.F., Archibald J.M., Keeling P.J. J. Mol. Biol. 348:1015-1024(2005) [PubMed: 15843030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CCMP449.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY826897 mRNA. Translation: AAW79358.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.39. 191640.
Family and domain databases
InterPro	IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Gene3D	G3DSA:3.20.20.110. RuBisCO_large. 1 hit. G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBL2_HETTR

Accession

Primary (citable) accession number: Q5ENN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	March 15, 2005
Last modified:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)