GenomeNet

Database: UniProt
Entry: K4HMJ2_GOSBA
LinkDB: K4HMJ2_GOSBA
Original site: K4HMJ2_GOSBA 
ID   K4HMJ2_GOSBA            Unreviewed;       179 AA.
AC   K4HMJ2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
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_00860};
GN   Synonyms=rbcS {ECO:0000256|HAMAP-Rule:MF_00859};
GN   ORFNames=ES319_A11G174000v1 {ECO:0000313|EMBL:KAB2057511.1};
OS   Gossypium barbadense (Sea-island cotton) (Egyptian cotton).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AFS41738.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3634 {ECO:0000313|EMBL:AFS41738.1};
RN   [1] {ECO:0000313|EMBL:AFS41738.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AD2-A-short-2 {ECO:0000313|EMBL:AFS41738.1};
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:KAB2057511.1, ECO:0000313|Proteomes:UP000327439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1400233.01 {ECO:0000313|EMBL:KAB2057511.1};
RA   Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA   Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA   Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA   Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA   Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT   "WGS assembly of Gossypium barbadense.";
RL   Submitted (JUN-2019) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JQ034269; AFS41738.1; -; Genomic_DNA.
DR   EMBL; CM018212; KAB2057511.1; -; Genomic_DNA.
DR   AlphaFoldDB; K4HMJ2; -.
DR   Proteomes; UP000327439; Chromosome a11.
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:AFS41738.1};
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   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;  20116 MW;  DE8465036B013E42 CRC64;
     MASSMISSAT IATASPAQAN MVTPFTGLKS ASAFPVTRKA NNDITSLASN GGRVQCMQVW
     PPTGKKKFET LSYLPDLTPV QLAKEVDYLL RSKWVPCLEF ELEEGFVHRK YSSLPTYYDG
     RYWTMWKLPM FGCTDSAQVL EELEECKKAY PNAFIRIIGF DNVRQVQCIS FIAYKPPGF
//
DBGET integrated database retrieval system