ID PYRB_PYRAB Reviewed; 308 AA.
AC P77918; G8ZHD2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Aspartate carbamoyltransferase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_00001};
DE EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001};
DE AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001};
DE Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001};
GN Name=pyrB {ECO:0000255|HAMAP-Rule:MF_00001}; OrderedLocusNames=PYRAB13270;
GN ORFNames=PAB1498;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=GE5 / Orsay;
RX PubMed=9209027; DOI=10.1128/jb.179.13.4143-4157.1997;
RA Purcarea C., Herve G., Ladjimi M.M., Cunin R.;
RT "Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon
RT Pyrococcus abyssi: genetic organization, structure, and expression in
RT Escherichia coli.";
RL J. Bacteriol. 179:4143-4157(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Catalyzes the condensation of carbamoyl phosphate and
CC aspartate to form carbamoyl aspartate and inorganic phosphate, the
CC committed step in the de novo pyrimidine nucleotide biosynthesis
CC pathway. {ECO:0000255|HAMAP-Rule:MF_00001}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00001};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_00001}.
CC -!- SUBUNIT: Heterooligomer of catalytic and regulatory chains.
CC {ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000269|PubMed:9209027}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001,
CC ECO:0000305}.
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DR EMBL; U61765; AAB62984.1; -; Genomic_DNA.
DR EMBL; AJ248287; CAB50232.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70769.1; -; Genomic_DNA.
DR PIR; C75042; C75042.
DR RefSeq; WP_010868442.1; NC_000868.1.
DR PDB; 1ML4; X-ray; 1.80 A; A=1-308.
DR PDBsum; 1ML4; -.
DR AlphaFoldDB; P77918; -.
DR SMR; P77918; -.
DR STRING; 272844.PAB1498; -.
DR GeneID; 1496715; -.
DR KEGG; pab:PAB1498; -.
DR PATRIC; fig|272844.11.peg.1412; -.
DR eggNOG; arCOG00911; Archaea.
DR HOGENOM; CLU_043846_1_2_2; -.
DR OrthoDB; 7792at2157; -.
DR PhylomeDB; P77918; -.
DR BRENDA; 2.1.3.2; 5242.
DR UniPathway; UPA00070; UER00116.
DR EvolutionaryTrace; P77918; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00670; asp_carb_tr; 1.
DR PANTHER; PTHR45753:SF6; ASPARTATE CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pyrimidine biosynthesis; Transferase.
FT CHAIN 1..308
FT /note="Aspartate carbamoyltransferase catalytic subunit"
FT /id="PRO_0000113253"
FT BINDING 57
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 58
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 86
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 107
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 135
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 168
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 229
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 268
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 269
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 16..36
FT /evidence="ECO:0007829|PDB:1ML4"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:1ML4"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:1ML4"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:1ML4"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1ML4"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:1ML4"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:1ML4"
SQ SEQUENCE 308 AA; 34901 MW; D36961E7749C012E CRC64;
MDWKGRDVIS IRDFSKEDIE TVLATAERLE RELKEKGQLE YAKGKILATL FFEPSTRTRL
SFESAMHRLG GAVIGFAEAS TSSVKKGESL RDTIKTVEQY CDVIVIRHPK EGAARLAAEV
AEVPVINAGD GSNQHPTQTL LDLYTIKKEF GRIDGLKIGL LGDLKYGRTV HSLAEALTFY
DVELYLISPE LLRMPRHIVE ELREKGMKVV ETTTLEDVIG KLDVLYVTRI QKERFPDEQE
YLKVKGSYQV NLKVLEKAKD ELRIMHPLPR VDEIHPEVDN TKHAIYFRQV FNGVPVRMAL
LALVLGVI
//
