PYRB_SULAC
ID PYRB_SULAC Reviewed; 299 AA.
AC Q55338; Q4J8H1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
GN Name=pyrB; OrderedLocusNames=Saci_1596;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=10447693; DOI=10.1046/j.1432-1327.1999.00619.x;
RA Durbecq V., Thia-Toong T.-L., Charlier D.R.M., Villeret V., Roovers M.,
RA Wattiez R., Legrain C., Glansdorff N.;
RT "Aspartate carbamoyltransferase from the thermoacidophilic archaeon
RT Sulfolobus acidocaldarius. Cloning, sequence analysis, enzyme purification
RT and characterization.";
RL Eur. J. Biochem. 264:233-241(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=12142413; DOI=10.1128/jb.184.16.4430-4441.2002;
RA Thia-Toong T.-L., Roovers M., Durbecq V., Gigot D., Glansdorff N.,
RA Charlier D.R.M.;
RT "Genes of de novo pyrimidine biosynthesis from the hyperthermoacidophilic
RT crenarchaeote Sulfolobus acidocaldarius: novel organization in a bipolar
RT operon.";
RL J. Bacteriol. 184:4430-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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 -!- SUBUNIT: Heterooligomer of catalytic and regulatory chains.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000305}.
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DR EMBL; X99872; CAA68165.1; -; Genomic_DNA.
DR EMBL; AJ459777; CAD31976.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80909.1; -; Genomic_DNA.
DR RefSeq; WP_011278411.1; NC_007181.1.
DR PDB; 1PG5; X-ray; 2.60 A; A=1-299.
DR PDB; 2BE9; X-ray; 2.60 A; A=1-299.
DR PDBsum; 1PG5; -.
DR PDBsum; 2BE9; -.
DR AlphaFoldDB; Q55338; -.
DR SMR; Q55338; -.
DR IntAct; Q55338; 1.
DR STRING; 330779.Saci_1596; -.
DR EnsemblBacteria; AAY80909; AAY80909; Saci_1596.
DR GeneID; 3474279; -.
DR KEGG; sai:Saci_1596; -.
DR PATRIC; fig|330779.12.peg.1536; -.
DR eggNOG; arCOG00911; Archaea.
DR HOGENOM; CLU_043846_1_2_2; -.
DR OMA; FPTEREY; -.
DR BRENDA; 2.1.3.2; 6160.
DR UniPathway; UPA00070; UER00116.
DR EvolutionaryTrace; Q55338; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
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 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..299
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113258"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:1PG5"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1PG5"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2BE9"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 278..297
FT /evidence="ECO:0007829|PDB:1PG5"
SQ SEQUENCE 299 AA; 34171 MW; 6A283A584F94E32D CRC64;
MKHIISAYNF SRDELEDIFA LTDKYSKNLN DTRKILSGKT ISIAFFEPST RTYLSFQKAI
INLGGDVIGF SGEESTSVAK GENLADTIRM LNNYSDGIVM RHKYDGASRF ASEISDIPVI
NAGDGKHEHP TQAVIDIYTI NKHFNTIDGL VFALLGDLKY ARTVNSLLRI LTRFRPKLVY
LISPQLLRAR KEILDELNYP VKEVENPFEV INEVDVLYVT RIQKERFVDE MEYEKIKGSY
IVSLDLANKM KKDSIILHPL PRVNEIDRKV DKTTKAKYFE QASYGVPVRM SILTKIYGE
