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Database: UniProt
Entry: A0A261FZ45_9BIFI
LinkDB: A0A261FZ45_9BIFI
Original site: A0A261FZ45_9BIFI 
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}.
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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
//
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