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Database: UniProt
Entry: N6XC17_9ACTO
LinkDB: N6XC17_9ACTO
Original site: N6XC17_9ACTO 
ID   N6XC17_9ACTO            Unreviewed;       332 AA.
AC   N6XC17;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
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   Name=argI {ECO:0000313|EMBL:ENO18723.1};
GN   ORFNames=HMPREF9004_0393 {ECO:0000313|EMBL:ENO18723.1};
OS   Schaalia cardiffensis F0333.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Schaalia.
OX   NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO18723.1, ECO:0000313|Proteomes:UP000013015};
RN   [1] {ECO:0000313|EMBL:ENO18723.1, ECO:0000313|Proteomes:UP000013015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0333 {ECO:0000313|EMBL:ENO18723.1,
RC   ECO:0000313|Proteomes:UP000013015};
RA   Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J., Forbes L.,
RA   Fowler G., Francisco L., Fu Q., Gibbs R., Gross S., Gubbala S., Hale W.,
RA   Hemphill L., Highlander S., Hirani K., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jayaseelan J.C., Jiang H., Joshi V., Korchina V., Kovar C.,
RA   Lara F., Lee S., Liu Y., Mata R., Mathew T., Munidasa M., Muzny D.,
RA   Nazareth L., Ngo R., Nguyen L., Nguyen N., Okwuonu G., Ongeri F.,
RA   Palculict T., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Qin X.,
RA   Qu J., Reid J., Ross M., Ruth R., Saada N., San Lucas F., Santibanez J.,
RA   Shang Y., Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J.,
RA   Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J.,
RA   Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.;
RT   "Reference genome for the Human Microbiome Project.";
RL   Submitted (MAR-2013) 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:ENO18723.1}.
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DR   EMBL; AQHZ01000007; ENO18723.1; -; Genomic_DNA.
DR   RefSeq; WP_005962124.1; NZ_KB822674.1.
DR   AlphaFoldDB; N6XC17; -.
DR   STRING; 888050.HMPREF9004_0393; -.
DR   PATRIC; fig|888050.3.peg.381; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_1_11; -.
DR   OrthoDB; 9802587at2; -.
DR   Proteomes; UP000013015; 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:SF2; 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|HAMAP-Rule:MF_01109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01109}.
FT   DOMAIN          8..148
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          156..328
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   BINDING         57..60
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         84
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         108
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         135..138
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         168
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         232
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         236..237
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         273..274
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         318
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   332 AA;  36437 MW;  E41E50D244E1DA2D CRC64;
     MTHPLHGRHL LREIDFTPAE WMSLIDLAAE LKAEKKEGRE VPRLKGRNIA LVFEKTSTRT
     RCSFEIAAAD QGAHTTFLDP TASQIGHKES VADTARVLGR LFDGIEYRGD EQAKVDTLAE
     LSGVPVWNGL TDDWHPTQML CDALTMREHA GKPLSEVSYA YVGDARFNTG RSLLVNGALI
     GADVRIVAPK QLWPDEECIA SAKKIAAETG ARITLTESVD EGVAGVDFVH TDIWVSMGEP
     KEVWDERIAL LSAYQVNAEL MAKAAPNAKF MHCLPAFHDR NTTIGEEIFQ ATGLGELEVT
     NEVFEGPASI VFDQAENRMH TIKAVMVATL GD
//
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