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Database: UniProt
Entry: A0A1H9DH33_9GAMM
LinkDB: A0A1H9DH33_9GAMM
Original site: A0A1H9DH33_9GAMM 
ID   A0A1H9DH33_9GAMM        Unreviewed;       144 AA.
AC   A0A1H9DH33;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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};
GN   Name=cbbS {ECO:0000256|HAMAP-Rule:MF_00859};
GN   ORFNames=SAMN04488038_10433 {ECO:0000313|EMBL:SEQ12701.1};
OS   Solimonas aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Solimonas.
OX   NCBI_TaxID=489703 {ECO:0000313|EMBL:SEQ12701.1, ECO:0000313|Proteomes:UP000199233};
RN   [1] {ECO:0000313|EMBL:SEQ12701.1, ECO:0000313|Proteomes:UP000199233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25927 {ECO:0000313|EMBL:SEQ12701.1,
RC   ECO:0000313|Proteomes:UP000199233};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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. 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_00859}.
CC   -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC       {ECO:0000256|ARBA:ARBA00038826, ECO:0000256|HAMAP-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}.
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DR   EMBL; FOFS01000004; SEQ12701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9DH33; -.
DR   STRING; 489703.SAMN04488038_10433; -.
DR   OrthoDB; 9788955at2; -.
DR   Proteomes; UP000199233; Unassembled WGS sequence.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; 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; IPR036385; RuBisCO_ssu_sf.
DR   PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31262:SF23; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT; 1.
DR   Pfam; PF00101; RuBisCO_small; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000199233}.
FT   DOMAIN          10..109
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
SQ   SEQUENCE   144 AA;  16657 MW;  7A5BB3AEF0F51184 CRC64;
     MMTNPMQRLT QGQFSFLPDL SDAEIKQQIE YGLEKGYAWS VEYTDDPHPR NTFWEMFGMP
     MFDLKDAAGV MMELAACRKT FPNHYIRMMA FDSTRNVESI TMSFIVNRPP SEPGFGLVRQ
     EVQGRSLRYT VQGYSSAKPE GERY
//
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