ID A0A2S5KUF5_9PROT Unreviewed; 336 AA.
AC A0A2S5KUF5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:PPC78343.1};
GN ORFNames=C4K68_05765 {ECO:0000313|EMBL:PPC78343.1};
OS Proteobacteria bacterium 228.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=2083153 {ECO:0000313|EMBL:PPC78343.1, ECO:0000313|Proteomes:UP000238196};
RN [1] {ECO:0000313|EMBL:PPC78343.1, ECO:0000313|Proteomes:UP000238196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=228 {ECO:0000313|EMBL:PPC78343.1,
RC ECO:0000313|Proteomes:UP000238196};
RA Krishnan R., Ramesh Kumar N.;
RT "novel marine gammaproteobacteria from coastal saline agro ecosystem.";
RL Submitted (FEB-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPC78343.1}.
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DR EMBL; PRLP01000016; PPC78343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5KUF5; -.
DR OrthoDB; 5289567at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000238196; 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: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 3: Inferred from homology;
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_00001}; Reference proteome {ECO:0000313|Proteomes:UP000238196};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00001}.
FT DOMAIN 18..162
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 171..316
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 70
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 71
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 98
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 120
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 150
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 153
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 183
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 238
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 279
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 280
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
SQ SEQUENCE 336 AA; 36768 MW; 051FCF9AAD394B45 CRC64;
MSHAAPHQLQ LNEQGQLRHF LTTEGLSREL LTDILDTAES FIDSNGRSVK KVPLMRGLTV
VNLFFENSTR TRSTFELAAQ KLSADILNLN ISTSATAKGE TLQDTLWNIR AMGADMFVVR
HADSGAAHFI AENVTPDVAI INAGDGRHAH PTQAMLDMLT IRRCKGEFGK LKVAIVGDIL
HSRVARSEIH ALNTLGAEEV RLIGPKTLVP DTLQALGANI YRDMKQGLKD VDVIVALRLQ
KERMNTALLP SESEFFRLYG LNEEKLAYAK PDAIVMHPGP INRGVEIESS VADGEQSRIL
TQVSNGIAVR MAVMSMAITG QLQQQQDLAK QQGAEG
//
