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Database: UniProt
Entry: K4HMN5_GOSAR
LinkDB: K4HMN5_GOSAR
Original site: K4HMN5_GOSAR 
ID   K4HMN5_GOSAR            Unreviewed;       179 AA.
AC   K4HMN5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00859, ECO:0000256|HAMAP-Rule:MF_00860};
DE   Includes:
DE     RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
DE              Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00859};
DE   Includes:
DE     RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00860};
GN   Name=rbcS {ECO:0000256|HAMAP-Rule:MF_00859};
GN   Synonyms=RBCS {ECO:0000256|HAMAP-Rule:MF_00860};
GN   ORFNames=F383_01218 {ECO:0000313|EMBL:KHG20485.1}, F383_17777
GN   {ECO:0000313|EMBL:KHG00063.1};
OS   Gossypium arboreum (Tree cotton) (Gossypium nanking).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AFS41722.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29729 {ECO:0000313|EMBL:AFS41722.1};
RN   [1] {ECO:0000313|EMBL:AFS41722.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A2-short-1 {ECO:0000313|EMBL:AFS41722.1}, and A2-short-2
RC   {ECO:0000313|EMBL:AFS41723.1};
RX   PubMed=22490824; DOI=10.1093/molbev/mss110;
RA   Gong L., Salmon A., Yoo M.J., Grupp K.K., Wang Z., Paterson A.H.,
RA   Wendel J.F.;
RT   "The cytonuclear dimension of allopolyploid evolution: an example from
RT   cotton using rubisco.";
RL   Mol. Biol. Evol. 29:3023-3036(2012).
RN   [2] {ECO:0000313|EMBL:KHG00063.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA   Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA   Wilkins T.A.;
RT   "G. arboreum L. cv. AKA8401 A2 genome assembly version 1.0.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000032142}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA   Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA   Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA   Wilkins T.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 in the photorespiration process. Both reactions occur
CC       simultaneously and in competition at the same active site. Although the
CC       small subunit is not catalytic it is essential for maximal activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00859}.
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. Although the small subunit is not catalytic it is
CC       essential for maximal activity. {ECO:0000256|HAMAP-Rule:MF_00860,
CC       ECO:0000256|RuleBase:RU003627}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00859, ECO:0000256|RuleBase:RU003627}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_00859}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {ECO:0000256|HAMAP-Rule:MF_00859}.
CC   -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00859, ECO:0000256|RuleBase:RU003627}.
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DR   EMBL; JQ034253; AFS41722.1; -; Genomic_DNA.
DR   EMBL; JQ034254; AFS41723.1; -; Genomic_DNA.
DR   EMBL; JRRC01110066; KHG00063.1; -; Genomic_DNA.
DR   EMBL; KN415836; KHG20485.1; -; Genomic_DNA.
DR   RefSeq; XP_017628098.1; XM_017772609.1.
DR   RefSeq; XP_017628337.1; XM_017772848.1.
DR   SMR; K4HMN5; -.
DR   GeneID; 108471042; -.
DR   GeneID; 108471228; -.
DR   KEGG; gab:108471042; -.
DR   KEGG; gab:108471228; -.
DR   OrthoDB; 5482775at2759; -.
DR   Proteomes; UP000032142; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd03527; RuBisCO_small; 1.
DR   Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 1.
DR   HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR   InterPro; IPR024681; RuBisCO_ssu.
DR   InterPro; IPR000894; RuBisCO_ssu_dom.
DR   InterPro; IPR024680; RuBisCO_ssu_N.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31262:SF29; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT 1A, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF12338; RbcS; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
DR   PRINTS; PR00152; RUBISCOSMALL.
DR   SMART; SM00961; RuBisCO_small; 1.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Chloroplast {ECO:0000256|HAMAP-Rule:MF_00859, ECO:0000313|EMBL:AFS41722.1};
KW   Photorespiration {ECO:0000256|ARBA:ARBA00023238, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_00859};
KW   Plastid {ECO:0000256|HAMAP-Rule:MF_00860, ECO:0000256|RuleBase:RU003627};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032142};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          67..176
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   179 AA;  20086 MW;  B5F478B5B996B463 CRC64;
     MASSMISSAT IATASPAQAN MVAPFTGLKS ASAFPVTRKA NNDITSLASN GGRVQCMQVW
     PPTGKKKFET LSYLPDLTPV QLAKEVDYLL RSKWVPCLEF ELEEGFVHRK YSSLPTYYDG
     RYWTMWKLPM FGCTDSAQVL EELEECKKAY PNAFIRIIGF DNVRQVQCIS FIAYKPPGF
//
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