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Database: UniProt
Entry: K9UZ64_9CYAN
LinkDB: K9UZ64_9CYAN
Original site: K9UZ64_9CYAN 
ID   K9UZ64_9CYAN            Unreviewed;       389 AA.
AC   K9UZ64;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   12-SEP-2018, entry version 28.
DE   SubName: Full=Ribulose-bisphosphate carboxylase {ECO:0000313|EMBL:AFZ00447.1};
DE            EC=4.1.1.39 {ECO:0000313|EMBL:AFZ00447.1};
GN   ORFNames=Cal6303_1394 {ECO:0000313|EMBL:AFZ00447.1};
OS   Calothrix sp. PCC 6303.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix.
OX   NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ00447.1, ECO:0000313|Proteomes:UP000010477};
RN   [1] {ECO:0000313|EMBL:AFZ00447.1, ECO:0000313|Proteomes:UP000010477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ00447.1,
RC   ECO:0000313|Proteomes:UP000010477};
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A.,
RA   Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X.,
RA   Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU003834}.
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DR   EMBL; CP003610; AFZ00447.1; -; Genomic_DNA.
DR   RefSeq; WP_015197096.1; NC_019751.1.
DR   ProteinModelPortal; K9UZ64; -.
DR   EnsemblBacteria; AFZ00447; AFZ00447; Cal6303_1394.
DR   KEGG; calt:Cal6303_1394; -.
DR   PATRIC; fig|1170562.3.peg.1517; -.
DR   KO; K08965; -.
DR   OrthoDB; POG091H0DKL; -.
DR   BioCyc; CSP1170562:G12V7-1343-MONOMER; -.
DR   Proteomes; UP000010477; Chromosome.
DR   GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:InterPro.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   InterPro; IPR017717; Diketo-Methiopentyl-P_enolase.
DR   InterPro; IPR033966; RuBisCO.
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; PTHR42704; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDF00157; 2_3-diketo-5-methylthiopentyl-; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000010477};
KW   Lyase {ECO:0000313|EMBL:AFZ00447.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010477}.
FT   DOMAIN       11    103       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      110    385       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
SQ   SEQUENCE   389 AA;  41532 MW;  B814FF2FFFD19193 CRC64;
     MSIEVDYRFP SGIDAEKQAK IIAVGQTAGT WDARFAHRQE SLQAHLAEVV SVVKLDGGDS
     VATVRFPESN VENDIPSLLT MIFGKYSMAG AAKVVDLRLP ENYGLRPKFG ISGIRNQLEI
     SQRPLIMAIF KPALGLSAQD HAEILQQVAQ AGLDIIKDDE ILGNIPTAPT FERLAACREV
     IDTVQQQTGR KLLYAVNVTG NATKLVENAR KLVRAGANAL LLNVFSYGFS VLEALAADPQ
     VNVPIFTHPA GAGAISAAPN HGISYPITLG TLMAHAGADA VLYPAHYGSL PFDANEEMMI
     RDRLRSRNVM PVPSAGIHPG IVPQALADYG KDVILNAGTG IMDHPDGAAA GVEAFFAALE
     RVQQGEPFDL ASLPEGALRN AIQKWGATK
//
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