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Database: UniProt
Entry: C8WMM1_EGGLE
LinkDB: C8WMM1_EGGLE
Original site: C8WMM1_EGGLE 
ID   C8WMM1_EGGLE            Unreviewed;       341 AA.
AC   C8WMM1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Ornithine carbamoyltransferase {ECO:0000313|EMBL:ACV54652.1};
GN   OrderedLocusNames=Elen_0670 {ECO:0000313|EMBL:ACV54652.1};
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:ACV54652.1, ECO:0000313|Proteomes:UP000001377};
RN   [1] {ECO:0000313|EMBL:ACV54652.1, 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   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. {ECO:0000256|RuleBase:RU003634}.
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DR   EMBL; CP001726; ACV54652.1; -; Genomic_DNA.
DR   RefSeq; WP_015760085.1; NC_013204.1.
DR   AlphaFoldDB; C8WMM1; -.
DR   STRING; 479437.Elen_0670; -.
DR   PaxDb; 479437-Elen_0670; -.
DR   KEGG; ele:Elen_0670; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_1_11; -.
DR   OrthoDB; 9802587at2; -.
DR   BioCyc; ELEN479437:G1GFY-678-MONOMER; -.
DR   Proteomes; UP000001377; Chromosome.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProt.
DR   GO; GO:0050231; F:putrescine carbamoyltransferase activity; IEA:InterPro.
DR   GO; GO:0033390; P:putrescine biosynthetic process from arginine via N-carbamoylputrescine; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   InterPro; IPR024903; PtcA.
DR   NCBIfam; TIGR00658; orni_carb_tr; 1.
DR   NCBIfam; TIGR04384; putr_carbamoyl; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
PE   3: Inferred from homology;
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001377};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          4..144
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          154..309
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
SQ   SEQUENCE   341 AA;  38409 MW;  0F763A48C1987A04 CRC64;
     MTVKDFLDTN DFTKDQLLDM IELSRVLKRC VKAGYYPELL KHKTLGMIFQ QVSTRTRLSF
     EGAMADLGGT GQFYAPGTIQ LGGHETIEDS ARVMSRLLDV LEARVDRHED LVELAKYATI
     PVINGMSDYN HPTQEMGDLL TMIEHLPEGK RIENCKMVFV GDATQVCVSE MFITSKMGMT
     FVQYGPEGHQ IREDLLEIGR KNCEVSGGSV SVTDNREEAM KDADFVYTDV WYGLYDKELS
     KDERMAIFYP TYQVTEELMA MAAPDAKFMH CLPASRGEEV TDAVIDGSQS ICWDEAENRK
     HSIRGLLAYF CKQAETDQTE AGEAHDQLNY LLEGLGKQAI K
//
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