ID Q6Y9B8_PROMN Unreviewed; 809 AA.
AC Q6Y9B8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 61.
DE RecName: Full=ribulose-bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00012287};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
DE Flags: Fragment;
GN Name=rbc3 {ECO:0000313|EMBL:AAO13079.1};
OS Prorocentrum minimum (Dinoflagellate) (Exuviaella minima).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Prorocentrales; Prorocentraceae;
OC Prorocentrum.
OX NCBI_TaxID=39449 {ECO:0000313|EMBL:AAO13079.1};
RN [1] {ECO:0000313|EMBL:AAO13079.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang H., Lin S.;
RT "Complex gene structure of the form II Rubisco in the dinoflagellate
RT Prorocentrum minimum (dinophyceae).";
RL J. Phycol. 39:1160-1171(2003).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate. Both reactions occur simultaneously and in competition at
CC the same active site. {ECO:0000256|ARBA:ARBA00003617}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC ChEBI:CHEBI:58272; EC=4.1.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00001067};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC ChEBI:CHEBI:58272; Evidence={ECO:0000256|ARBA:ARBA00000537};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC subfamily. {ECO:0000256|ARBA:ARBA00005475}.
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DR EMBL; AY169231; AAO13079.1; -; mRNA.
DR AlphaFoldDB; Q6Y9B8; -.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd08211; RuBisCO_large_II; 1.
DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 2.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR InterPro; IPR020871; RuBisCO_lsuII.
DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 2.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 2.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 2.
PE 2: Evidence at transcript level;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AAO13079.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plastid {ECO:0000256|ARBA:ARBA00022640}.
FT DOMAIN 2..266
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT DOMAIN 334..454
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 467..772
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAO13079.1"
SQ SEQUENCE 809 AA; 88072 MW; 8AB4B0A725BA0DE0 CRC64;
QGGDFIKNDE PQGNQTFCQM NECIPEVVKA MRAAQEETGQ GKLFSANITA DDPNEMIARA
KYILNQMGPM AENCAFLVDG YVAGGTAVTV ARRNFPKQFL HYHRAGHGAV TSPQTQRGYT
AFVHTKLSRV IGASGIHTGT MSFGKMEGDA SDKNIGFMLQ DDVADGPYYR QEWEGMKQTT
PIISGGMNAL RLPAFFENLG HSNVILTAGG GAFGHKDGPK QGAISCAQGE ESWKLWKAGT
YGDVSLSDGV VEYAKTHEEL KGAFLTFQKD ADQIYPGWKE KLGYTGESSV QAASFNWQKK
DLAAAFVGAS TTRKASSVAR RALDQSSRYA DLSLTEEDLI KNGQHVLVAY IMKPKAGYDY
LATAAHFAAE SSTGTNVNVC TTDDFTKTVD ALVYYIDPEN EEMKIAYPTA LFDRNITDGR
AMMCSVLTLS IGNNQGMGDV DYGKIYDIYF PPQYLRLFDG PSCCVIDMWR ILGRGTVGGG
LVVGTIIKPK LGLQPKPFGQ ACYGFWQGGD FIKNDEPQGN QTFCQMNECI PEVVKAMRAA
QEETGQGKLF SANITADDPN EMIARAKYIL NQMGPMAENC AFLVDGYVAG GTAVTVARRN
FPKQFLHYHR AGHGAVTSPQ TQRGYTAFVH TKLSRVIGAS GIHTGTMSFG KMEGDASDKN
IGFMLQDDVA DGPYYRQEWE GMKQTTPIIS GGMNALRLPA FFENLGHSNV ILTAGGGAFG
HKDGPKQGAI SCAQGEESWK LWKAGTYGDV SLSDGVVEYA KTHEELKGAF LTFQKDADQI
YPGWKEKLGY TGESSVQAAS FNWQKKELS
//
