OTC_MYCS2
ID OTC_MYCS2 Reviewed; 307 AA.
AC A0QYS8; I7G3K5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000303|PubMed:3566963};
DE Short=OTCase {ECO:0000303|PubMed:3566963};
DE EC=2.1.3.3 {ECO:0000305|PubMed:3566963};
GN Name=argF {ECO:0000303|PubMed:3566963};
GN OrderedLocusNames=MSMEG_3772, MSMEI_3683;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION AS AN OTCASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 14468;
RX PubMed=3566963; DOI=10.1139/o86-177;
RA Ahmad S., Bhatnagar R.K., Venkitasubramanian T.A.;
RT "Ornithine transcarbamylase from Mycobacterium smegmatis ATCC 14468:
RT purification, properties, and reaction mechanism.";
RL Biochem. Cell Biol. 64:1349-1355(1986).
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:3566963}.
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; Evidence={ECO:0000305|PubMed:3566963};
CC -!- ACTIVITY REGULATION: Inhibited by arginine, norvaline.
CC {ECO:0000269|PubMed:3566963}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 mM for carbamoyl phosphate {ECO:0000269|PubMed:3566963};
CC KM=0.25 mM for L-ornithine {ECO:0000269|PubMed:3566963};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01109}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; CP000480; ABK75220.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40142.1; -; Genomic_DNA.
DR RefSeq; WP_011729314.1; NZ_SIJM01000005.1.
DR RefSeq; YP_888066.1; NC_008596.1.
DR AlphaFoldDB; A0QYS8; -.
DR SMR; A0QYS8; -.
DR STRING; 246196.MSMEI_3683; -.
DR EnsemblBacteria; ABK75220; ABK75220; MSMEG_3772.
DR EnsemblBacteria; AFP40142; AFP40142; MSMEI_3683.
DR GeneID; 66735142; -.
DR KEGG; msg:MSMEI_3683; -.
DR KEGG; msm:MSMEG_3772; -.
DR PATRIC; fig|246196.19.peg.3711; -.
DR eggNOG; COG0078; Bacteria.
DR OMA; DGNNVCN; -.
DR OrthoDB; 988597at2; -.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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-UniRule.
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.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_1000073030"
FT BINDING 50..53
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 77
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 101
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 128..131
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 160
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 224
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 228..229
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 264..265
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 292
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ SEQUENCE 307 AA; 33388 MW; 355FD07788911954 CRC64;
MIRHFLRDDD LSPEEQAEVL TLAADLKKTP FSRRPLEGPR GVAVIFEKNS TRTRFSFEMG
IAQLGGHAIV VDGRSTQLGR EETLEDTGAV LSRYVDAIVW RTFAQERLTA MASGASVPIV
NALSDEFHPC QVLADLQTLA ERKGKLAGLR MTYFGDGANN MAHSLMLGGV TAGVHVTIAA
PDGFEPDPRF VDAARRRAAE TGATVALTKD AKAGADGADV LVTDTWTSMG QENDGLDRVR
PFRPFQVNAD LLELADPAAV VLHCLPAHRG HEITDEVIDG PQSAVFDEAE NRLHAQKALL
VWLLEKR
