ID A0A261FZ45_9BIFI Unreviewed; 144 AA.
AC A0A261FZ45;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Aspartate carbamoyltransferase {ECO:0000313|EMBL:OZG64193.1};
GN ORFNames=BHAP_1360 {ECO:0000313|EMBL:OZG64193.1};
OS Bifidobacterium hapali.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630172 {ECO:0000313|EMBL:OZG64193.1, ECO:0000313|Proteomes:UP000216074};
RN [1] {ECO:0000313|EMBL:OZG64193.1, ECO:0000313|Proteomes:UP000216074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100202 {ECO:0000313|EMBL:OZG64193.1,
RC ECO:0000313|Proteomes:UP000216074};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG64193.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MWWY01000025; OZG64193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FZ45; -.
DR OrthoDB; 5599321at2; -.
DR Proteomes; UP000216074; 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-KW.
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 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 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Transferase {ECO:0000313|EMBL:OZG64193.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..93
FT /note="Aspartate carbamoyltransferase regulatory subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01948"
FT DOMAIN 100..142
FT /note="Aspartate carbamoyltransferase regulatory subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02748"
SQ SEQUENCE 144 AA; 15973 MW; B2A379DF4E17B8B4 CRC64;
MEVTSIVNGI IIDHVPAGTA LKVLDYLKIN PAKTKLALIM NTDSHLYGTK DIIKIEDEDG
KKTPSIDLDV LGLVARTATV GIVRGGTIVE KKTPTLPEHV VNILTCKNPR CVTTTERGID
QMFHLTHSER QEYRCDYCDE EAKL
//