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Database: UniProt
Entry: Q4C1R1_CROWT
LinkDB: Q4C1R1_CROWT
Original site: Q4C1R1_CROWT 
ID   Q4C1R1_CROWT            Unreviewed;       472 AA.
AC   Q4C1R1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   12-SEP-2018, entry version 66.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338};
GN   Name=cbbL {ECO:0000256|HAMAP-Rule:MF_01338};
GN   Synonyms=rbcL {ECO:0000256|HAMAP-Rule:MF_01338};
GN   ORFNames=CwatDRAFT_2714 {ECO:0000313|EMBL:EAM50081.1};
OS   Crocosphaera watsonii WH 8501.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM50081.1, ECO:0000313|Proteomes:UP000003922};
RN   [1] {ECO:0000313|EMBL:EAM50081.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM50081.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   DOE Joint Genome Institute;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAM50081.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM50081.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M.;
RT   "Annotation of the draft genome assembly of Crocosphaera watsonii WH
RT   8501.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAM50081.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM50081.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Crocosphaera watsonii
RT   WH 8501.";
RL   Submitted (JUN-2005) 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.
CC       {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose
CC       1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|HAMAP-
CC       Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate =
CC       D-ribulose 1,5-bisphosphate + O(2). {ECO:0000256|HAMAP-
CC       Rule:MF_01338}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC       disulfide-linked. The disulfide link is formed within the large
CC       subunit homodimers. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- PTM: The disulfide bond which can form in the large chain dimeric
CC       partners within the hexadecamer appears to be associated with
CC       oxidative stress and protein turnover. {ECO:0000256|HAMAP-
CC       Rule:MF_01338}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a "head-to-tail" conformation. In form I
CC       RuBisCO this homodimer is arranged in a barrel-like tetramer with
CC       the small subunits forming a tetrameric "cap" on each end of the
CC       "barrel". {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01338}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAM50081.1}.
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DR   EMBL; AADV02000039; EAM50081.1; -; Genomic_DNA.
DR   RefSeq; WP_007306215.1; NZ_AADV02000039.1.
DR   ProteinModelPortal; Q4C1R1; -.
DR   EnsemblBacteria; EAM50081; EAM50081; CwatDRAFT_2714.
DR   KEGG; cwa:CwatDRAFT_2714; -.
DR   KO; K01601; -.
DR   OrthoDB; POG091H14UZ; -.
DR   Proteomes; UP000003922; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   CDD; cd08212; RuBisCO_large_I; 1.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 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   InterPro; IPR020888; RuBisCO_lsuI.
DR   PANTHER; PTHR42704; PTHR42704; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003922};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000313|EMBL:EAM50081.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Photorespiration {ECO:0000256|HAMAP-Rule:MF_01338};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003922}.
FT   DOMAIN       20    139       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      150    459       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
FT   ACT_SITE    171    171       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   ACT_SITE    290    290       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       197    197       Magnesium; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   METAL       199    199       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   METAL       200    200       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     119    119       Substrate; in homodimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   BINDING     169    169       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     173    173       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     291    291       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     323    323       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   BINDING     375    375       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01338}.
FT   SITE        330    330       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
FT   MOD_RES     197    197       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01338}.
FT   DISULFID    243    243       Interchain; in linked form.
FT                                {ECO:0000256|HAMAP-Rule:MF_01338}.
SQ   SEQUENCE   472 AA;  52505 MW;  387ABF66579BF98C CRC64;
     MPQATKAGFN AGVQDYRLTY YTPDYTPKDT DLLACFRMTP QPGVPPEEAG AAVAAESSTG
     TWTTVWTDNL TDLDRYKGRC YDIEPVPNED NQYFCFIAYP LDLFEEGSVT NVLTSLVGNV
     FGFKALRALR LEDIRFPVAL IKTFQGPPHG ITVERDKLNK YGRPLLGCTI KPKLGLSAKN
     YGRAVYECLR GGLDFTKDDE NINSQPFMRW RDRFLFVQEA IEKSQAETNE VKGHYLNVTA
     GTCEEMMKRA EFAKEIGTPI VMHDFITGGF TANTTLAKYC RDNGLLLHIH RAMHAVIDRQ
     KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGERGITMG FVDLMREDYV EEDRSRGIFF
     TQDYASMPGT MPVASGGIHV WHMPALVEIF GDDSCLQFGG GTLGHPWGNA PGATANRVAL
     EACIQARNEG RSLSGEAGNQ VIREACKWSP ELAAACELWK EIKFEFEAMD TL
//
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