ID A0A3P1VZI9_9FUSO Unreviewed; 151 AA.
AC A0A3P1VZI9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000256|HAMAP-Rule:MF_00002};
GN Name=pyrI {ECO:0000256|HAMAP-Rule:MF_00002};
GN ORFNames=EII29_08965 {ECO:0000313|EMBL:RRD39008.1};
OS Leptotrichia sp. OH3620_COT-345.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=2491048 {ECO:0000313|EMBL:RRD39008.1, ECO:0000313|Proteomes:UP000280115};
RN [1] {ECO:0000313|EMBL:RRD39008.1, ECO:0000313|Proteomes:UP000280115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH3620_COT-345 {ECO:0000313|EMBL:RRD39008.1,
RC ECO:0000313|Proteomes:UP000280115};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in allosteric regulation of aspartate
CC carbamoyltransferase. {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|HAMAP-
CC Rule:MF_00002}.
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:RRD39008.1}.
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DR EMBL; RQYW01000015; RRD39008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1VZI9; -.
DR OrthoDB; 5599321at2; -.
DR Proteomes; UP000280115; 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}; Transferase {ECO:0000313|EMBL:RRD39008.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00002}.
FT DOMAIN 3..93
FT /note="Aspartate carbamoyltransferase regulatory subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01948"
FT DOMAIN 98..146
FT /note="Aspartate carbamoyltransferase regulatory subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02748"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
SQ SEQUENCE 151 AA; 17100 MW; AA4C92E349594B9F CRC64;
MELQITALKN GIVIDHIPIE KTFPIVEILH LREYGEIVTV ACNLKSSSLG KKGLIKIEDR
SLGENELGEI AILAPDVTIN IIENFKVVKK IKLAIPNEIT GLIKCNNNKC ISNHEEIESK
FIKIVDEDKI KYKCFYCERV IAENEIELKP L
//
