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Database: UniProt
Entry: A0A418UVY9_9ACTO
LinkDB: A0A418UVY9_9ACTO
Original site: A0A418UVY9_9ACTO 
ID   A0A418UVY9_9ACTO        Unreviewed;       336 AA.
AC   A0A418UVY9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=argF {ECO:0000313|EMBL:RJF44748.1};
GN   ORFNames=D4740_00770 {ECO:0000313|EMBL:RJF44748.1};
OS   Actinomyces sp. 2119.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=2321393 {ECO:0000313|EMBL:RJF44748.1, ECO:0000313|Proteomes:UP000284680};
RN   [1] {ECO:0000313|EMBL:RJF44748.1, ECO:0000313|Proteomes:UP000284680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2119 {ECO:0000313|EMBL:RJF44748.1,
RC   ECO:0000313|Proteomes:UP000284680};
RA   Li J.;
RL   Submitted (SEP-2018) 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:RJF44748.1}.
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DR   EMBL; QYRR01000001; RJF44748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418UVY9; -.
DR   Proteomes; UP000284680; 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; 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:UP000284680};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01109}.
FT   DOMAIN          9..149
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          157..330
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   BINDING         58..61
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         85
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         109
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         136..139
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         169
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         233
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         237..238
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         275..276
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         320
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   336 AA;  37283 MW;  83D23FDF72BB37A5 CRC64;
     MTHHPLHNRS FLKELDFTAE EWKSLLDLSA QLKADKKAGR EVRRLVGKNI ALIFEKTSTR
     TRCSFEVAAY DQGAQVTYLD PSGSQMGHKE SVADTARVLG RFYDGIEFRG KKQEHVEQLA
     ALSGVPVWNG LTDEWHPTQM LADQLTMLEH SGKPIEEISF AYLGDARNNV ANSLLVAAAL
     TGMDVRMVAP VELQTPPEVV AEAQRLAESS GARILITDNV AKGVAGVDFL YTDVWVSMGE
     AKEVWDERIA LLRPYQVNAA LVETTGNPDV KFLHCLPAFH DRNTTVGEDI FVKTGMDGLE
     VTDDVFESEH NVAFDQAENR MHTIKAVMVA TLGEWD
//
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