ID Q1HMN4_9PHAE Unreviewed; 392 AA.
AC Q1HMN4;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=rbcL {ECO:0000313|EMBL:ABF19625.1};
OS Dictyota ciliolata.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Dictyotales; Dictyotaceae; Dictyota.
OX NCBI_TaxID=381671 {ECO:0000313|EMBL:ABF19625.1};
RN [1] {ECO:0000313|EMBL:ABF19625.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HV632 {ECO:0000313|EMBL:ABF19625.1};
RA De Clerck O., Leliaert F., Verbruggen H., Lane C.E., Campos De Paula J.,
RA Payo D.A., Coppejans E.;
RT "A revised classification of the Dictyoteae (Dictyotales, Phaeophyceae)
RT based on rbcL and 26S ribosomal DNA sequence analyses.";
RL J. Phycol. 42:1271-1288(2006).
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};
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DR EMBL; DQ472053; ABF19625.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1HMN4; -.
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 Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
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 PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDG01052; RuBisCO; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 4: Predicted;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
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..101
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 111..389
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:ABF19625.1"
FT NON_TER 392
FT /evidence="ECO:0000313|EMBL:ABF19625.1"
SQ SEQUENCE 392 AA; 43098 MW; CC343BDA5E616EDE CRC64;
PQPGVDPVEA AAAVAGESST ATWTVVWTDL LTACDIYRAK AYRVDPVPGT NDQFFAYIAY
ECDLFEEGSL ANLTASIIGN VFGFKAVKAL RLEDMRIPFA YLKTFQGPAT GVIVERERLD
KFGRPLLGAT VKPKLGLSGK NYGRVVYEGL RGGLDFLKDD ENINSQPFMR WKERFLYCME
GVNRAAAATG EVKGSYLNVT AATMENMYER ADYANSLGTV IVMIDLVIGY TAIQTMAIWA
RKAQMILHLH RAGNSTYARQ KNHGINFRVI CKWMRMSGVD HIHAGTVVGK LEGDPLMVRG
FYNTLLLTEL KVNLAEGLFF DMDWASLRKC VPVASGGIHC GQMHQLLYYL GDDVVLQFGG
GTIGHPDGIQ SGATANRVAL EAMVLARNEG RD
//
