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2YYT

Crystal structure of uncharacterized conserved protein from Geobacillus kaustophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
A0005829cellular_componentcytosol
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0044205biological_process'de novo' UMP biosynthetic process
B0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
B0005829cellular_componentcytosol
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0016831molecular_functioncarboxy-lyase activity
B0044205biological_process'de novo' UMP biosynthetic process
C0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
C0005829cellular_componentcytosol
C0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0016831molecular_functioncarboxy-lyase activity
C0044205biological_process'de novo' UMP biosynthetic process
D0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
D0005829cellular_componentcytosol
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0016831molecular_functioncarboxy-lyase activity
D0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00156
Number of Residues14
DetailsOMPDECASE Orotidine 5'-phosphate decarboxylase active site. VFlDlKlhDIPnTV
ChainResidueDetails
AVAL58-VAL71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01200
ChainResidueDetails
ALYS63
BLYS63
CLYS63
DLYS63

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01200
ChainResidueDetails
AASP12
BLYS34
BASP61
BTHR124
BARG186
BGLN195
BGLY215
BARG216
CASP12
CLYS34
CASP61
ALYS34
CTHR124
CARG186
CGLN195
CGLY215
CARG216
DASP12
DLYS34
DASP61
DTHR124
DARG186
AASP61
DGLN195
DGLY215
DARG216
ATHR124
AARG186
AGLN195
AGLY215
AARG216
BASP12

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
AASP61
ALYS63

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
BASP61
BLYS63

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
CASP61
CLYS63

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
DASP61
DLYS63

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
AASP61
ALYS34
ALYS63
AASP66

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
BASP61
BLYS34
BLYS63
BASP66

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
CASP61
CLYS34
CLYS63
CASP66

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
DASP61
DLYS34
DLYS63
DASP66

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PDB entries from 2024-07-17

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