ID A0A3R9M893_9RHOB Unreviewed; 318 AA.
AC A0A3R9M893;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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 ORFNames=EJA01_10525 {ECO:0000313|EMBL:RSK32764.1};
OS Rhodovulum robiginosum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=68292 {ECO:0000313|EMBL:RSK32764.1, ECO:0000313|Proteomes:UP000275159};
RN [1] {ECO:0000313|EMBL:RSK32764.1, ECO:0000313|Proteomes:UP000275159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12329 {ECO:0000313|EMBL:RSK32764.1,
RC ECO:0000313|Proteomes:UP000275159};
RA Gupta D., Guzman M.S., Bose A.;
RT "Draft genome sequence of a marine photoferrotrophic bacterium, Rhodovulum
RT robiginosum.";
RL Submitted (DEC-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 -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC produce L-citrulline. {ECO:0000256|ARBA:ARBA00003822}.
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:RSK32764.1}.
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DR EMBL; RWGU01000048; RSK32764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9M893; -.
DR OrthoDB; 9774690at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000275159; 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:UP000275159};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00001}.
FT DOMAIN 6..148
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 157..302
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 58
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 59
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 86
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 108
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 139
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 169
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 223
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 264
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
FT BINDING 265
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001"
SQ SEQUENCE 318 AA; 34974 MW; D0B445F614EE8D9A CRC64;
MTFRARHLLG IEHLKPDDIR CILDLSEHYV GLNRQPVKHA DALEGLTQIN MFFEASTRTQ
ASFELAGKRL GADVMNMAMQ ASSLKKGETL IDTALTLNAM HPDLLVVRHP QSGAVDLLAQ
KVHCAVLNAG DGRHEHPTQA LLDALTIRRA KGRLQRLTVA ICGDIAHSRV ARSNILLLGK
MENRVRLIGP PTLIPARAAE FGVEVYDDMK EGLAGADVVM MLRLQKERMD GAFIPSEREY
YHRFGLDADK LAFAKDDAIV MHPGPMNRGV EIDGTLADDI NRSVIQEQVE MGVAVRMAAM
DLLARNLRAT LSQGAGHV
//
