ID A0A0G4JSJ1_9GAMM Unreviewed; 154 AA.
AC A0A0G4JSJ1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000256|ARBA:ARBA00021764, ECO:0000256|HAMAP-Rule:MF_00002};
GN Name=pyrI {ECO:0000256|HAMAP-Rule:MF_00002};
GN ORFNames=BN1221_01051 {ECO:0000313|EMBL:CPR14644.1};
OS Brenneria goodwinii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=1109412 {ECO:0000313|EMBL:CPR14644.1, ECO:0000313|Proteomes:UP000044377};
RN [1] {ECO:0000313|Proteomes:UP000044377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBR1 {ECO:0000313|Proteomes:UP000044377};
RA Paterson Steve;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in allosteric regulation of aspartate
CC carbamoyltransferase. {ECO:0000256|ARBA:ARBA00002565,
CC ECO:0000256|HAMAP-Rule:MF_00002}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00002};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00002};
CC -!- SUBUNIT: Contains catalytic and regulatory chains. {ECO:0000256|HAMAP-
CC Rule:MF_00002}.
CC -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000256|ARBA:ARBA00010498,
CC ECO:0000256|HAMAP-Rule:MF_00002}.
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DR EMBL; CGIG01000001; CPR14644.1; -; Genomic_DNA.
DR RefSeq; WP_048636411.1; NZ_MJLY01000012.1.
DR AlphaFoldDB; A0A0G4JSJ1; -.
DR STRING; 1109412.BN1221_01051; -.
DR OrthoDB; 5599321at2; -.
DR Proteomes; UP000044377; Unassembled WGS sequence.
DR GO; GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.20; Aspartate carbamoyltransferase regulatory subunit, C-terminal domain; 1.
DR Gene3D; 3.30.70.140; Aspartate carbamoyltransferase regulatory subunit, N-terminal domain; 1.
DR HAMAP; MF_00002; Asp_carb_tr_reg; 1.
DR InterPro; IPR020545; Asp_carbamoyltransf_reg_N.
DR InterPro; IPR002801; Asp_carbamoylTrfase_reg.
DR InterPro; IPR020542; Asp_carbamoyltrfase_reg_C.
DR InterPro; IPR036792; Asp_carbatrfase_reg_C_sf.
DR InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR NCBIfam; TIGR00240; ATCase_reg; 1.
DR PANTHER; PTHR35805; ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN; 1.
DR PANTHER; PTHR35805:SF1; ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN; 1.
DR Pfam; PF01948; PyrI; 1.
DR Pfam; PF02748; PyrI_C; 1.
DR SUPFAM; SSF57825; Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain; 1.
DR SUPFAM; SSF54893; Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00002};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_00002}; Reference proteome {ECO:0000313|Proteomes:UP000044377};
KW Transferase {ECO:0000313|EMBL:CPR14644.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00002}.
FT DOMAIN 7..95
FT /note="Aspartate carbamoyltransferase regulatory subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01948"
FT DOMAIN 103..150
FT /note="Aspartate carbamoyltransferase regulatory subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02748"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
SQ SEQUENCE 154 AA; 17493 MW; 4A0E1B51B60392AF CRC64;
MTHDNKLQVE AIKRGTVIDH IPAQVGFKLL TLFKLTATDQ RITIGLNLPS NQLGRKDLIK
IENVFLTEQQ ANQLAIYAPQ ATVNQIDDYD VVRKLSPTLP DHIDDVLTCP NSNCISRIEP
VSSSFSVKLR DDEVQLKCKY CEKEFERQAV LQDR
//
