ID A0A0P0FQJ0_9BACE Unreviewed; 153 AA.
AC A0A0P0FQJ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000256|HAMAP-Rule:MF_00002};
GN Name=pyrI {ECO:0000256|HAMAP-Rule:MF_00002,
GN ECO:0000313|EMBL:ALJ57333.1};
GN ORFNames=BcellWH2_00057 {ECO:0000313|EMBL:ALJ57333.1}, DWW88_18015
GN {ECO:0000313|EMBL:RGU24235.1}, DWX97_08840
GN {ECO:0000313|EMBL:RGS37833.1}, F2Y53_25490
GN {ECO:0000313|EMBL:KAA5433337.1}, F2Y70_19870
GN {ECO:0000313|EMBL:KAA5424121.1}, F2Y81_20335
GN {ECO:0000313|EMBL:KAA5414440.1}, F2Y86_19380
GN {ECO:0000313|EMBL:KAA5405543.1}, F2Y87_10915
GN {ECO:0000313|EMBL:KAA5419476.1};
OS Bacteroides cellulosilyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=246787 {ECO:0000313|EMBL:ALJ57333.1, ECO:0000313|Proteomes:UP000061809};
RN [1] {ECO:0000313|EMBL:ALJ57333.1, ECO:0000313|Proteomes:UP000061809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH2 {ECO:0000313|EMBL:ALJ57333.1,
RC ECO:0000313|Proteomes:UP000061809};
RX PubMed=26430127;
RA Wu M., McNulty N.P., Rodionov D.A., Khoroshkin M.S., Griffin N.W.,
RA Cheng J., Latreille P., Kerstetter R.A., Terrapon N., Henrissat B.,
RA Osterman A.L., Gordon J.I.;
RT "Genetic determinants of in vivo fitness and diet responsiveness in
RT multiple human gut Bacteroides.";
RL Science 350:AAC5992-AAC5992(2015).
RN [2] {ECO:0000313|Proteomes:UP000283341, ECO:0000313|Proteomes:UP000285677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF17-25 {ECO:0000313|EMBL:RGU24235.1,
RC ECO:0000313|Proteomes:UP000285677}, and AF22-3AC
RC {ECO:0000313|EMBL:RGS37833.1, ECO:0000313|Proteomes:UP000283341};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000325055, ECO:0000313|Proteomes:UP000425249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A2 {ECO:0000313|EMBL:KAA5433337.1,
RC ECO:0000313|Proteomes:UP000425249}, BIOML-A3
RC {ECO:0000313|EMBL:KAA5424121.1, ECO:0000313|Proteomes:UP000475645},
RC BIOML-A6 {ECO:0000313|EMBL:KAA5414440.1,
RC ECO:0000313|Proteomes:UP000448877}, BIOML-A7
RC {ECO:0000313|EMBL:KAA5405543.1, ECO:0000313|Proteomes:UP000325055},
RC and BIOML-A8 {ECO:0000313|EMBL:KAA5419476.1,
RC ECO:0000313|Proteomes:UP000482653};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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}.
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DR EMBL; CP012801; ALJ57333.1; -; Genomic_DNA.
DR EMBL; VVYW01000018; KAA5405543.1; -; Genomic_DNA.
DR EMBL; VVYV01000041; KAA5414440.1; -; Genomic_DNA.
DR EMBL; VVYX01000011; KAA5419476.1; -; Genomic_DNA.
DR EMBL; VVYT01000079; KAA5424121.1; -; Genomic_DNA.
DR EMBL; VVYS01000985; KAA5433337.1; -; Genomic_DNA.
DR EMBL; QRVJ01000005; RGS37833.1; -; Genomic_DNA.
DR EMBL; QRXS01000011; RGU24235.1; -; Genomic_DNA.
DR RefSeq; WP_007214025.1; NZ_VVYX01000011.1.
DR AlphaFoldDB; A0A0P0FQJ0; -.
DR STRING; 246787.BcellWH2_00057; -.
DR GeneID; 69508375; -.
DR KEGG; bcel:BcellWH2_00057; -.
DR PATRIC; fig|246787.4.peg.60; -.
DR eggNOG; COG1781; Bacteria.
DR Proteomes; UP000061809; Chromosome.
DR Proteomes; UP000283341; Unassembled WGS sequence.
DR Proteomes; UP000285677; Unassembled WGS sequence.
DR Proteomes; UP000325055; Unassembled WGS sequence.
DR Proteomes; UP000425249; Unassembled WGS sequence.
DR Proteomes; UP000448877; Unassembled WGS sequence.
DR Proteomes; UP000475645; Unassembled WGS sequence.
DR Proteomes; UP000482653; 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:ALJ57333.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00002}.
FT DOMAIN 8..98
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 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT BINDING 115
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 153 AA; 17320 MW; 913CC6281D6D1891 CRC64;
MSEKKQELQV AALENGTVID HIPSENLFTV VSLLGLEHMN NNITIGFNLK SGKLGTKGII
KIADKFFCDD EINRIAVVAP NVKLNIIRDY EVVEKREVSL PEELRGIVKC ANPKCITNNE
PMATLFHVVD KENCVIRCHY CEKEQNRNEI EII
//
