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Database: UniProt
Entry: J0LL28_9BIFI
LinkDB: J0LL28_9BIFI
Original site: J0LL28_9BIFI 
ID   J0LL28_9BIFI            Unreviewed;       344 AA.
AC   J0LL28;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Ornithine carbamoyltransferase {ECO:0000256|ARBA:ARBA00013007, ECO:0000256|HAMAP-Rule:MF_01109};
DE            Short=OTCase {ECO:0000256|HAMAP-Rule:MF_01109};
DE            EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007, ECO:0000256|HAMAP-Rule:MF_01109};
GN   ORFNames=HMPREF9156_00992 {ECO:0000313|EMBL:EJD64497.1};
OS   Scardovia wiggsiae F0424.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Scardovia.
OX   NCBI_TaxID=857290 {ECO:0000313|EMBL:EJD64497.1, ECO:0000313|Proteomes:UP000006415};
RN   [1] {ECO:0000313|EMBL:EJD64497.1, ECO:0000313|Proteomes:UP000006415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0424 {ECO:0000313|EMBL:EJD64497.1,
RC   ECO:0000313|Proteomes:UP000006415};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA   Baranova O.V., Blanton J.M., Tanner A.C., Mathney J., Dewhirst F.E.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C.,
RA   Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Scardovia wiggsiae F0424.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC         phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:58228; EC=2.1.3.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001065, ECO:0000256|HAMAP-
CC         Rule:MF_01109};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805,
CC       ECO:0000256|HAMAP-Rule:MF_01109}.
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:EJD64497.1}.
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DR   EMBL; AGZS01000006; EJD64497.1; -; Genomic_DNA.
DR   RefSeq; WP_007148056.1; NZ_JH719940.1.
DR   AlphaFoldDB; J0LL28; -.
DR   STRING; 857290.HMPREF9156_00992; -.
DR   GeneID; 84815915; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_1_11; -.
DR   OrthoDB; 9802587at2; -.
DR   Proteomes; UP000006415; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   HAMAP; MF_01109; OTCase; 1.
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; IPR024904; OTCase_ArgI.
DR   NCBIfam; TIGR00658; orni_carb_tr; 1.
DR   PANTHER; PTHR45753:SF1; ORNITHINE CARBAMOYLTRANSFERASE, CATABOLIC; 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; PR00102; OTCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006415};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01109}.
FT   DOMAIN          14..154
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          160..334
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   BINDING         63..66
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         90
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         114
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         141..144
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         173
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         237
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         241..242
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         279..280
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         324
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   344 AA;  38235 MW;  0DB2B5913A613DC8 CRC64;
     METATASENV FQGRSFLACK DFTPAEIMYL VDFALHLKRL KKDHIPHRYL EGKNIALLFE
     KTSTRTRSAF VTAANDLGAF PEFMGADSTQ LGKKESIEDT ARVLGSMFDG IEYRGFAHSD
     VEALARNAGV PVWNGLTDEW HPTQMIADLM TVKEKFGRLK GLTLTFVGDG RNNMANSLLV
     AGTMAGINVR ILAPKELQPS GEVVSIAGQF ARQTGARYLV TDDIDEGVRG ANIIYTDVWV
     SMGEDNWEER IGLLAPYTVT LDMMRRTGTP DGELIFLHCL PAFHDVKTAY GKEIFEKFGM
     AEMEVTDEVF RSDLSWQFVQ AENRMHSIKA IMAATLGNLF IPSV
//
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