ID   B0KA36_THEP3            Unreviewed;       304 AA.
AC   B0KA36;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   18-JUN-2025, entry version 95.
DE   RecName: Full=Aspartate carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_00001};
DE            EC=2.1.3.2 {ECO:0000256|HAMAP-Rule:MF_00001};
DE   AltName: Full=Aspartate transcarbamylase {ECO:0000256|HAMAP-Rule:MF_00001};
DE            Short=ATCase {ECO:0000256|HAMAP-Rule:MF_00001};
GN   Name=pyrB {ECO:0000256|HAMAP-Rule:MF_00001};
GN   OrderedLocusNames=Teth39_1345 {ECO:0000313|EMBL:ABY94999.1};
OS   Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS   thermohydrosulfuricum).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY94999.1, ECO:0000313|Proteomes:UP000002156};
RN   [1] {ECO:0000313|Proteomes:UP000002156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33223 / DSM 2355 / 39E
RC   {ECO:0000313|Proteomes:UP000002156};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA   Richardson P.;
RT   "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00043884, ECO:0000256|HAMAP-
CC       Rule:MF_00001}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate +
CC         phosphate + H(+); 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         Evidence={ECO:0000256|ARBA:ARBA00048859, ECO:0000256|HAMAP-
CC         Rule:MF_00001};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852, ECO:0000256|HAMAP-Rule:MF_00001}.
CC   -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC       organized as two trimers (C3), and six regulatory PyrI chains organized
CC       as three dimers (R2). {ECO:0000256|HAMAP-Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000256|ARBA:ARBA00008896,
CC       ECO:0000256|HAMAP-Rule:MF_00001}.
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DR   EMBL; CP000924; ABY94999.1; -; Genomic_DNA.
DR   RefSeq; WP_003868401.1; NC_010321.1.
DR   AlphaFoldDB; B0KA36; -.
DR   STRING; 340099.Teth39_1345; -.
DR   KEGG; tpd:Teth39_1345; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_0_9; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000002156; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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-UniRule.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   FunFam; 3.40.50.1370:FF:000007; Aspartate carbamoyltransferase; 1.
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   NCBIfam; NF002032; PRK00856.1; 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   3: Inferred from homology;
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_00001}; Reference proteome {ECO:0000313|Proteomes:UP000002156};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00001}.
FT   DOMAIN          4..146
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          152..298
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   BINDING         55
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         56
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         83
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         105
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         133
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         136
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         166
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         220
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         261
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT   BINDING         262
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
SQ   SEQUENCE   304 AA;  33926 MW;  5447707779263214 CRC64;
     MKRKDLLGIK DLSKEEILEV LDTAKEMKKI LNGEKYSQIL KGKTVVTIFF EPSTRTRLSF
     EMAAKYLGAH YGNIEVATSS VAKGESLIDT IRTVEMMKAD VIITRHNMSG APHLMAKYTN
     ASIINAGDGI NEHPTQALLD MMTIREKKES FEGLKVAIIG DIMHSRVARS NIWGLKKMGA
     EVRVAGPSTL MPPAIEKLGV KAYYNVEEAI EGADVVMGLR IQLERQKSGL FPSIDEYREY
     FGINKERMKL AKPDAILMHP GPINRNVELT SEAANDKYSV IEEQVTNGVA VRMALLKILC
     ERRN
//