OTC_MORAB
ID OTC_MORAB Reviewed; 301 AA.
AC Q9K4Y9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000303|PubMed:10692366};
DE Short=OTCase {ECO:0000303|PubMed:10692366};
DE EC=2.1.3.3 {ECO:0000269|PubMed:12644485};
GN Name=argF {ECO:0000303|PubMed:10692366};
OS Moritella abyssi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=111292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2693;
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).
RN [2]
RP PROTEIN SEQUENCE OF 1-6, FUNCTION AS AN OTCASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=2693;
RX PubMed=12644485; DOI=10.1128/jb.185.7.2161-2168.2003;
RA Xu Y., Feller G., Gerday C., Glansdorff N.;
RT "Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to
RT low temperatures in ornithine carbamoyltransferase from Moritella abyssi.";
RL J. Bacteriol. 185:2161-2168(2003).
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, which is a substrate for argininosuccinate
CC synthetase, the enzyme involved in the final step in arginine
CC biosynthesis. {ECO:0000269|PubMed:12644485}.
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:0000269|PubMed:12644485};
CC -!- ACTIVITY REGULATION: Inhibited by excess of arginine and by the
CC bisubstrate delta-N-phosphonoacetyl-L-ornithine (PALO).
CC {ECO:0000269|PubMed:12644485}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 mM for carbamoyl phosphate (at pH 9 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:12644485};
CC KM=1 mM for carbamoyl phosphate (at pH 9 and at 20 degrees Celsius)
CC {ECO:0000269|PubMed:12644485};
CC KM=1.1 mM for carbamoyl phosphate (at pH 9 and at 5 degrees Celsius)
CC {ECO:0000269|PubMed:12644485};
CC KM=1.78 mM for L-ornithine (at pH 9 and at 5 degrees Celsius)
CC {ECO:0000269|PubMed:12644485};
CC KM=8 mM for L-ornithine (at pH 9 and at 20 degrees Celsius)
CC {ECO:0000269|PubMed:12644485};
CC KM=45 mM for L-ornithine (at pH 9 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:12644485};
CC Note=kcat is 15 and 766 sec(-1) at 30 degrees Celsius and pH 9 for L-
CC ornithine and carbamoyl phosphate, respectively. kcat is 87 and 694
CC sec(-1) at 20 degrees Celsius and pH 9 for L-ornithine and carbamoyl
CC phosphate, respectively. kcat is 132 and 214 sec(-1) at 5 degrees
CC Celsius and pH 9 for L-ornithine and carbamoyl phosphate,
CC respectively.;
CC pH dependence:
CC Optimum pH is between 9 and 10. {ECO:0000269|PubMed:12644485};
CC Temperature dependence:
CC Optimum temperature is between 23 and 25 degrees Celsius. 37% of this
CC maximal activity could still be observed at 5 degrees Celsius.
CC {ECO:0000269|PubMed:12644485};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000305}.
CC -!- SUBUNIT: The enzyme is present as a mixture of trimers and dodecamers,
CC with the relative proportions of the two forms depending on the salt
CC concentration. In addition, the trimeric fraction could reassociate
CC into dodecamers when the salt concentration is increased. It appears
CC that in vivo, the main fraction is in the dodecameric form.
CC {ECO:0000269|PubMed:12644485}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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.
CC {ECO:0000305|PubMed:12644485}.
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DR EMBL; AJ252021; CAB95022.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9K4Y9; -.
DR SMR; Q9K4Y9; -.
DR SABIO-RK; Q9K4Y9; -.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Direct protein sequencing; Transferase.
FT CHAIN 1..301
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000112948"
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; 32870 MW; 83BCEB6A72CDCE83 CRC64;
MENLLSVKDL SKQQILDLLA LAKAVKANPA EYSQALAGKS IVTIYEKPSL RTRVTFDIGI
HKLGGHAVYL DAQNGAIGER ETVKDFAANI SRWADAIVAR VVSHKTLEGL VEHGSVPVVN
SLCDLYHPCQ ALADFLTISE HYEDVSKVKL AYVGEGNNVT HSLMLTGAIL GAEVTAVCPR
GSSPDAQIVK QAMALAEISG GKINVTDNLD DIVDYDVIYG DTWVSMGDDT PLAQVKEKYM
PYQINKALLM RTGIKHVLHC QPAHRELEIT SEVMDGEHSL IFDQAENRMH AQNAVLLTLL
K
