ID A0A2T3N0Q7_9GAMM Unreviewed; 334 AA.
AC A0A2T3N0Q7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:PSW05790.1};
GN ORFNames=C9I89_08665 {ECO:0000313|EMBL:PSW05790.1};
OS Photobacterium lipolyticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=266810 {ECO:0000313|EMBL:PSW05790.1, ECO:0000313|Proteomes:UP000240904};
RN [1] {ECO:0000313|EMBL:PSW05790.1, ECO:0000313|Proteomes:UP000240904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16190 {ECO:0000313|EMBL:PSW05790.1,
RC ECO:0000313|Proteomes:UP000240904};
RA Butler K.;
RT "Whole genome sequencing of Histamine producing bacteria.";
RL Submitted (MAR-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:PSW05790.1}.
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DR EMBL; PYMC01000004; PSW05790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3N0Q7; -.
DR OrthoDB; 9802587at2; -.
DR Proteomes; UP000240904; 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:UP000240904};
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 158..330
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 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 334 AA; 37499 MW; 697072649FB55364 CRC64;
MAFNLRNRNF LKLLDFTPRE IQHLLELSAE LKKAKYSGYE QPRLTGKNIA LIFEKSSTRT
RCAFEVAAYD QGAKVSYLGP SGSQIGHKES MKDTARVLGR MYDGIEYRGF GQEIVEELGA
YAGVPVWNGL TDEFHPTQIL ADFLTMQEHS RGKPLHKTTF AYLGDARNNM GNSLMVGAAK
MGMDIRLVAP KTFWPEADLV AQCQDIAKHT GAKITLTDKV KEGVKGCDFL YTDVWVSMGE
SKDAWDERVK LMTPYQINMD IIKATGNPHV KFMHCLPAFH NDETTVGAEV AEKYNMKGLE
VTEDVFESEY SIVFDEAENR MHTIKAIMVA TLGD
//
