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Database: UniProt
Entry: C8WHP9_EGGLE
LinkDB: C8WHP9_EGGLE
Original site: C8WHP9_EGGLE 
ID   C8WHP9_EGGLE            Unreviewed;       314 AA.
AC   C8WHP9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Aspartate carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_00001};
DE            EC=2.1.3.2 {ECO:0000256|HAMAP-Rule:MF_00001};
DE   AltName: Full=Aspartate transcarbamylase {ECO:0000256|HAMAP-Rule:MF_00001};
DE            Short=ATCase {ECO:0000256|HAMAP-Rule:MF_00001};
GN   Name=pyrB {ECO:0000256|HAMAP-Rule:MF_00001};
GN   OrderedLocusNames=Elen_1674 {ECO:0000313|EMBL:ACV55640.1};
OS   Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS   KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=479437 {ECO:0000313|EMBL:ACV55640.1, ECO:0000313|Proteomes:UP000001377};
RN   [1] {ECO:0000313|EMBL:ACV55640.1, ECO:0000313|Proteomes:UP000001377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 /
RC   NCTC 11813 / VPI 0255 / 1899 B {ECO:0000313|Proteomes:UP000001377};
RX   PubMed=21304654; DOI=10.4056/sigs.33592;
RA   Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT   0255).";
RL   Stand. Genomic Sci. 1:174-182(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001363, ECO:0000256|HAMAP-
CC         Rule:MF_00001};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852, ECO:0000256|HAMAP-Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000256|HAMAP-Rule:MF_00001}.
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DR   EMBL; CP001726; ACV55640.1; -; Genomic_DNA.
DR   RefSeq; WP_009307088.1; NC_013204.1.
DR   AlphaFoldDB; C8WHP9; -.
DR   STRING; 479437.Elen_1674; -.
DR   PaxDb; 479437-Elen_1674; -.
DR   GeneID; 69511060; -.
DR   KEGG; ele:Elen_1674; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_0_11; -.
DR   OMA; FPTEREY; -.
DR   OrthoDB; 9774690at2; -.
DR   BioCyc; ELEN479437:G1GFY-1683-MONOMER; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000001377; Chromosome.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   NCBIfam; TIGR00670; asp_carb_tr; 1.
DR   PANTHER; PTHR45753:SF6; ASPARTATE CARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_00001}; Reference proteome {ECO:0000313|Proteomes:UP000001377};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00001}.
FT   DOMAIN          6..149
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          156..303
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
SQ   SEQUENCE   314 AA;  34556 MW;  959A486A9026F7C7 CRC64;
     MAFNHKHLID ITEYSADDIM TVLETAVRFK EVNERRIKQV PTLKGVTVVN MFNEPSTRTR
     SSFEIAEKRL SANSLNFGGS STSTVKGESL VDTVETLCAY KIDMIIVRDK HAGVPRKIAD
     VSGAHVIDAG DGKHQHPTQA LLDLYSIWEV KGDLNGLKVG VVGDIGHSRV CGSLIPALKI
     MGCEVTVVAP PTLLPARPDI LGADHVTTKL DEALPDLDVV YMLRIQRERL EGAPYPSLRE
     YNMLYGLTKD REHLMKPDAL ICHPGPINRG VELDSYMADH PKRSVILDQV YAGILTRMAE
     MYLLLGGSED GLTA
//
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