PYRB_AQUAE
ID PYRB_AQUAE Reviewed; 291 AA.
AC O66726;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
GN Name=pyrB; OrderedLocusNames=aq_409;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2;
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06675.1; -; Genomic_DNA.
DR PIR; B70337; B70337.
DR RefSeq; NP_213286.1; NC_000918.1.
DR RefSeq; WP_010880224.1; NC_000918.1.
DR PDB; 3D6N; X-ray; 2.30 A; B=1-291.
DR PDB; 4BJH; X-ray; 2.20 A; B=1-291.
DR PDBsum; 3D6N; -.
DR PDBsum; 4BJH; -.
DR AlphaFoldDB; O66726; -.
DR SMR; O66726; -.
DR STRING; 224324.aq_409; -.
DR EnsemblBacteria; AAC06675; AAC06675; aq_409.
DR KEGG; aae:aq_409; -.
DR PATRIC; fig|224324.8.peg.336; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_0_0; -.
DR InParanoid; O66726; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 1844275at2; -.
DR BRENDA; 2.1.3.2; 396.
DR UniPathway; UPA00070; UER00116.
DR EvolutionaryTrace; O66726; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR PANTHER; PTHR11405:SF16; PTHR11405:SF16; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..291
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113087"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:4BJH"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4BJH"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3D6N"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:4BJH"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:4BJH"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3D6N"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:3D6N"
FT HELIX 271..289
FT /evidence="ECO:0007829|PDB:4BJH"
SQ SEQUENCE 291 AA; 33558 MW; 93523D3DBDD01534 CRC64;
MRSLISSLDL TREEVEEILK YAKEFKEGKE ETIKASAVLF FSEPSTRTRL SFEKAARELG
IETYLVSGSE SSTVKGESFF DTLKTFEGLG FDYVVFRVPF VFFPYKEIVK SLNLRLVNAG
DGTHQHPSQG LIDFFTIKEH FGEVKDLRVL YVGDIKHSRV FRSGAPLLNM FGAKIGVCGP
KTLIPRDVEV FKVDVFDDVD KGIDWADVVI WLRLQKERQK ENYIPSESSY FKQFGLTKER
FEKVKLYMHP GPVNRNVDID HELVYTEKSL IQEQVKNGIP VRKAIYKFLW T
