ID A0A1I4TR32_9PROT Unreviewed; 316 AA.
AC A0A1I4TR32;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ECO:0000313|EMBL:CAE6493158.1};
GN ORFNames=DEO56_11475 {ECO:0000313|EMBL:HBZ31191.1}, NMYAN_120096
GN {ECO:0000313|EMBL:CAE6493158.1}, SAMN05421880_1346
GN {ECO:0000313|EMBL:SFM79003.1};
OS Nitrosomonas nitrosa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=52442 {ECO:0000313|EMBL:SFM79003.1, ECO:0000313|Proteomes:UP000199561};
RN [1] {ECO:0000313|EMBL:SFM79003.1, ECO:0000313|Proteomes:UP000199561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm146 {ECO:0000313|EMBL:SFM79003.1,
RC ECO:0000313|Proteomes:UP000199561};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HBZ31191.1, ECO:0000313|Proteomes:UP000264024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBA8641 {ECO:0000313|EMBL:HBZ31191.1};
RX PubMed=30148503; DOI=.1038/nbt.4229;
RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A.,
RA Chaumeil P.A., Hugenholtz P.;
RT "A standardized bacterial taxonomy based on genome phylogeny substantially
RT revises the tree of life.";
RL Nat. Biotechnol. 36:996-1004(2018).
RN [3] {ECO:0000313|EMBL:CAE6493158.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nitrosomonas nitrosa 18-3D {ECO:0000313|EMBL:CAE6493158.1};
RA Han P.;
RL Submitted (FEB-2021) 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|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001363, 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}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805}.
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DR EMBL; CAJNAP010000004; CAE6493158.1; -; Genomic_DNA.
DR EMBL; DOVE01000301; HBZ31191.1; -; Genomic_DNA.
DR EMBL; FOUF01000034; SFM79003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4TR32; -.
DR STRING; 52442.SAMN05421880_1346; -.
DR OrthoDB; 9774690at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000199561; Unassembled WGS sequence.
DR Proteomes; UP000264024; Unassembled WGS sequence.
DR Proteomes; UP000601736; Unassembled WGS sequence.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-EC.
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 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 3: Inferred from homology;
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_00001}; Reference proteome {ECO:0000313|Proteomes:UP000199561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00001}.
FT DOMAIN 14..158
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 166..312
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 66
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 67
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 94
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 116
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 146
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 149
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 179
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 234
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 275
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 276
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
SQ SEQUENCE 316 AA; 34904 MW; F69C93E7AF5E51AF CRC64;
MNRNPQLNKQ GELQHLLTTE GLPISILRHI LDTAESFAGV TEREVKKIPL LRGKSVFNLF
FEPSTRTRTT FEIAAKRLSA DVINLNIAVS AQSKGETLLD TVNNLSAMHA DMFVVRHAQS
GAAHMIASHV RPDIHVINAG DGRHAHPTQA LLDMFTIRRY KQDFHNLRVA IVGDILHSRV
ARSQIHALTT LGVPEVRVIA PKTILPSKVE RLGVHVYHDM AQGLKDIDVL IMLRLQNERM
VGASLPSSEE YFKYYGLTQE KLAMAKPDAI VMHPGPMNRG VEIDSAVADG KQSVILPQVT
FGIAVRMAVM SILAGN
//
