ID Q6Y9H6_PROMN Unreviewed; 1057 AA.
AC Q6Y9H6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 62.
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=rbcC10 {ECO:0000313|EMBL:AAO13030.1};
OS Prorocentrum minimum (Dinoflagellate) (Exuviaella minima).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Prorocentrales; Prorocentraceae;
OC Prorocentrum.
OX NCBI_TaxID=39449 {ECO:0000313|EMBL:AAO13030.1};
RN [1] {ECO:0000313|EMBL:AAO13030.1}
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; AY169173; AAO13030.1; -; mRNA.
DR AlphaFoldDB; Q6Y9H6; -.
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; 3.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 2.
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; 3.
DR Pfam; PF02788; RuBisCO_large_N; 2.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 3.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 2.
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:AAO13030.1};
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 1..161
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT DOMAIN 229..349
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 362..667
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT DOMAIN 735..855
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 868..1056
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:AAO13030.1"
FT NON_TER 1057
FT /evidence="ECO:0000313|EMBL:AAO13030.1"
SQ SEQUENCE 1057 AA; 114880 MW; 97A78ED1A99018E1 CRC64;
GHGAVTSPQT QRGYTAFVHT KLSRVIGASG IHTGTMSFGK MEGDASDKNI GFMLQDDVAD
GPYYRQEWEG MKQTTPIISG GMNALRLPAF FENLGHSNVI LTAGGGAFGH KDGPKQGAIS
CAQGEESWKL WKAGTYGDVS LSDGVVEYAK THEELKGAFL TFQKDADQIY PGWKEKLGYT
GESSVQAASF NWQKKDLAAA FVGASTTRKA SSVARRALDQ SSRYADLSLT EEDLIKNGQH
VLVAYIMKPK AGYDYLATAA HFAAESSTGT NVNVCTTDDF TKTVDALVYY IDPENEEMKI
AYPTALFDRN ITDGRAMMCS VLTLSIGNNQ GMGDVDYGKI YDIYFPPQYL RLFDGPSCCV
IDMWRILGRG TVGGGLVVGT IIKPKLGLQP KPFGQACYGF WQGGDFIKND EPQGNQTFCQ
MNECIPEVVK AMRAAQEETG QGKLFSANIT ADDPNEMIAR AKYILNQMGP MAENCAFLVD
GYVAGGTAVT VARRNFPKQF LHYHRAGHGA VTSPQTQRGY TAFVHTKLSR VIGASGIHTG
TMSFGKMEGD ASDKNIGFML QDDVADGPYY RQEWEGMKQT TPIISGGMNA LRLPAFFENL
GHSNVILTAG GGAFGHKDGP KQGAISCAQG EESWKLWKAG TYGDVSLSDG VVEYAKTHEE
LKGAFLTFQK DADQIYPGWK EKLGYTGESS VQAASFNWQK KDLAAAFVGA SKARKASSVT
RRALDQSSRY ADLSLTEEDL IKNGQHVLVA YIMKPKAGYD YLATAAHFAA ESSTGTNVNV
CTTDDFTKTV DALVYYIDPE NEEMKIAYPT ALFDRNITDG RAMMCSVLTL SIGNNQGMGD
VDYGKIYDIY FPPQYLRLFD GPSCCVIDMW RILGRGTVGG GLVVGTIIKP KLGLQPKPFG
QACYGFWQGG DFIKNDEPQG NQTFCQMNEC IPEVVKAMRA AQEETGQGKL FSANITADDP
NEMIARAKYI LNQMGPMAEN CAFLVDGYVA GGTAVTVARR NFPKQFLHYH RAGHGAVTSP
QTQRGYTAFV HTKLSRVIGA SGIHTGTMSF GKMEGDA
//
