ID C8WQ56_ALIAD Unreviewed; 411 AA.
AC C8WQ56;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Ribulose-bisphosphate carboxylase {ECO:0000313|EMBL:ACV57160.1};
DE EC=4.1.1.39 {ECO:0000313|EMBL:ACV57160.1};
GN OrderedLocusNames=Aaci_0096 {ECO:0000313|EMBL:ACV57160.1};
OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 /
OS DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 /
OS NRRL B-14509 / 104-IA) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV57160.1, ECO:0000313|Proteomes:UP000001917};
RN [1] {ECO:0000313|Proteomes:UP000001917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC {ECO:0000313|Proteomes:UP000001917};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT acidocaldarius DSM 446.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV57160.1, ECO:0000313|Proteomes:UP000001917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC {ECO:0000313|Proteomes:UP000001917};
RX PubMed=21304673; DOI=10.4056/sigs.591104;
RA Mavromatis K., Sikorski J., Lapidus A., Glavina Del Rio T., Copeland A.,
RA Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Meincke L.,
RA Sims D., Chertkov O., Han C., Brettin T., Detter J.C., Wahrenburg C.,
RA Rohde M., Pukall R., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Alicyclobacillus acidocaldarius type strain
RT (104-IA).";
RL Stand. Genomic Sci. 2:9-18(2010).
RN [3] {ECO:0007829|PDB:4NAS}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 3-408 IN COMPLEX WITH CALCIUM.
RA Tan K., Li H., Clancy S., Joachimiak A.;
RT "The crystal structure of a rubisco-like protein (MtnW) from
RT Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446.";
RL Submitted (OCT-2013) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC {ECO:0000256|RuleBase:RU003834}.
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DR EMBL; CP001727; ACV57160.1; -; Genomic_DNA.
DR RefSeq; WP_012809551.1; NC_013205.1.
DR PDB; 4NAS; X-ray; 1.92 A; A/B/C/D=3-408.
DR PDBsum; 4NAS; -.
DR AlphaFoldDB; C8WQ56; -.
DR SMR; C8WQ56; -.
DR STRING; 521098.Aaci_0096; -.
DR KEGG; aac:Aaci_0096; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_9; -.
DR Proteomes; UP000001917; 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 CDD; cd08209; RLP_DK-MTP-1-P-enolase; 1.
DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4NAS};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Calcium {ECO:0007829|PDB:4NAS}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Lyase {ECO:0000313|EMBL:ACV57160.1}; Metal-binding {ECO:0007829|PDB:4NAS};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000001917}.
FT DOMAIN 10..116
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 128..407
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4NAS"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4NAS"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4NAS"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4NAS"
SQ SEQUENCE 411 AA; 44279 MW; B0539CCF19ECAFEA CRC64;
MVNQDSSPRD AVVATYRLRD RKDKLEARAE GIAVGLTIGT WTDLPAARKS EVAKHCGRVE
GIRVLDERPD GDVVAEIDIA YPVANLNGTF ASLLVTVFGK LSMDGEIRLE RLQMPDELVR
QFPGPKFGVE GVRRRLGAYN RPLVMSIFKA CAGLTLDELV EAFGEQAEGG VDLVKDDEIF
FTEAYATPED RVRAYAAKAD EIAQRTGRRT AYAVNLTGPV HSLRERARRL AELGAGALLV
NVVAYGYDVV ADLARDPDVD VPILAHPAVS GALYGSPNYG IAADIVLGQL MRLAGADIGI
FPSMYGSVTL GREATDRLLQ HLRAEGPHKP VLPAPSAGIY PGLVPRLYQD FGVDLVLNAG
GGIHGHPGGA RMGGRAFFDA IWAVEHGVPL EEAAKDRPAL RQALEKWGMP S
//
