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Database: UniProt/TrEMBL
Entry: E3HQ31_ACHXA
LinkDB: E3HQ31_ACHXA
Original site: E3HQ31_ACHXA 
ID   E3HQ31_ACHXA            Unreviewed;       425 AA.
AC   E3HQ31;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   28-FEB-2018, entry version 44.
DE   SubName: Full=Ribulose bisphosphate carboxylase large chain, catalytic domain protein {ECO:0000313|EMBL:ADP17189.1};
DE            EC=4.1.1.39 {ECO:0000313|EMBL:ADP17189.1};
GN   OrderedLocusNames=AXYL_03869 {ECO:0000313|EMBL:ADP17189.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP17189.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP17189.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP17189.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading
RT   bacterium Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU003834}.
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DR   EMBL; CP002287; ADP17189.1; -; Genomic_DNA.
DR   RefSeq; WP_013394503.1; NC_014640.1.
DR   ProteinModelPortal; E3HQ31; -.
DR   STRING; 762376.AXYL_03869; -.
DR   EnsemblBacteria; ADP17189; ADP17189; AXYL_03869.
DR   KEGG; axy:AXYL_03869; -.
DR   PATRIC; fig|762376.5.peg.3884; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; AHFPFIA; -.
DR   OrthoDB; POG091H2GZ2; -.
DR   BioCyc; AXYL762376:G1GOM-3846-MONOMER; -.
DR   Proteomes; UP000006876; Chromosome.
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   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000006876};
KW   Lyase {ECO:0000313|EMBL:ADP17189.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006876}.
FT   DOMAIN       15    131       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      141    421       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
SQ   SEQUENCE   425 AA;  45591 MW;  45AFBF21D457815F CRC64;
     MNSQSFTATY LIETPLDPAK VAEVMAGEQS CGTFTRVQGE TDELRARARA RIESIETLES
     AAAPSLPNAW LARQPGGMPG LYRRARVRIA FPVANVGASL PTLAATVGGN LYDLGEVTGL
     RLESMELPAN YRAQFDVPRV GIAGTRQLTG VAHGPLVGTI IKPNVGLSPE QTAHLAAQLC
     AAGVDFIKDD EVCANPAHAP LAQRVAAVMA VVRAHRERTG RQVMVAFNIS DETDAMRRHA
     DLIEREGGTC VMASLNHCGY SAIQTLRRST PLALHGHRNG YGALSRHPLL GLGFQAYQTL
     WRLAGVDHMH VHGLQGKFSQ EDAEVVESAR DCLASLTLGI DDPVMPAFSS GQWAGTVPAT
     WAAVRSDDLL FMSGGGILAH PDGPAAGVLS IRQAWQAMRD GERLEDYARN APELRRAIEC
     FGHRA
//
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