ID   OTC_MORPR               Reviewed;         301 AA.
AC   Q9K4Z4;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=argF;
OS   Moritella profunda.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=111291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2674;
RX   PubMed=10692366; DOI=10.1128/jb.182.6.1609-1615.2000;
RA   Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N.;
RT   "Evolution of arginine biosynthesis in the bacterial domain: novel gene-
RT   enzyme relationships from psychrophilic Moritella strains (Vibrionaceae)
RT   and evolutionary significance of N-alpha-acetyl ornithinase.";
RL   J. Bacteriol. 182:1609-1615(2000).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC       carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC       produce L-citrulline. {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 1/3.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved threonine and leucine residues in
CC       positions 50 and 261, respectively, which are part of the
CC       carbamoylphosphate and ornithine binding sites; they are replaced by a
CC       leucine and a glutamine residue, respectively. {ECO:0000305}.
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DR   EMBL; AJ252020; CAB95016.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9K4Z4; -.
DR   SMR; Q9K4Z4; -.
DR   UniPathway; UPA00068; UER00112.
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   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1370; -; 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   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00658; orni_carb_tr; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Transferase.
FT   CHAIN           1..301
FT                   /note="Ornithine carbamoyltransferase"
FT                   /id="PRO_0000112949"
FT   BINDING         100
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         127..130
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         158
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         221
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         225..226
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         260
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000305"
FT   BINDING         288
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   301 AA;  32987 MW;  E713A381359A098A CRC64;
     MENLLSVKDL SKQQILDLLA LAKAVKANPA EYSQALAGKS IVTIYEKQSL RTRVTFDIGI
     HKLGGHAVYL DAQNGAIGER ETVKDFAANI SRWADAIVAR VMSHKTLEGL VEHGSVPVVN
     SLCDLYHPCQ ALADFLTISE HYEDVSKVKL AYIGEGNNVT HSLMLTGAIL GAEVTAVCPR
     GSSPDAQIVK QAMALAEISG GKINVTDNLD DIVDYDVIYG DTWVSMGDDT PLAQVKEKYM
     PYQINKELLI RTGIKHVLHC QPAHRELEIT SEVMDGEHSL IFDQAENRMH AQNAVLLTLL
     K