OTC2_ECOLI
ID OTC2_ECOLI Reviewed; 334 AA.
AC P06960; P78308; Q2MCE9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Ornithine carbamoyltransferase subunit F {ECO:0000303|PubMed:789338};
DE Short=OTCase-2 {ECO:0000303|PubMed:789338};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=argF {ECO:0000303|PubMed:789338}; OrderedLocusNames=b0273, JW0266;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6382166; DOI=10.1093/nar/12.15.6277;
RA van Vliet F., Cunin R., Jacobs A., Piette J., Gigot D., Lauwereys M.,
RA Pierard A., Glansdorff N.;
RT "Evolutionary divergence of genes for ornithine and aspartate carbamoyl-
RT transferases -- complete sequence and mode of regulation of the Escherichia
RT coli argF gene; comparison of argF with argI and pyrB.";
RL Nucleic Acids Res. 12:6277-6289(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-41.
RX PubMed=3968036; DOI=10.1128/jb.161.2.714-719.1985;
RA Falmagne P., Portetelle D., Stalon V.;
RT "Immunological and structural relatedness of catabolic ornithine
RT carbamoyltransferases and the anabolic enzymes of enterobacteria.";
RL J. Bacteriol. 161:714-719(1985).
RN [6]
RP SUBUNIT.
RX PubMed=4558857; DOI=10.1111/j.1432-1033.1972.tb01814.x;
RA Legrain C., Halleux P., Stalon V., Glansdorff N.;
RT "The dual genetic control of ornithine carbamolytransferase in Escherichia
RT coli. A case of bacterial hybrid enzymes.";
RL Eur. J. Biochem. 27:93-102(1972).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=789338; DOI=10.1128/jb.128.1.35-38.1976;
RA Legrain C., Stalon V., Glansdorff N.;
RT "Escherichia coli ornithine carbamolytransferase isoenzymes: evolutionary
RT significance and the isolation of lambdaargF and lambdaargI transducing
RT bacteriophages.";
RL J. Bacteriol. 128:35-38(1976).
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:789338}.
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:0000255|HAMAP-
CC Rule:MF_01109};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.02 mM for carbamoyl phosphate {ECO:0000269|PubMed:789338};
CC KM=5 mM for L-ornithine {ECO:0000269|PubMed:789338};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000305}.
CC -!- SUBUNIT: In E.coli strain K12, trimer of identical or non-identical
CC chains are composed of ArgI (I) and/or ArgF (F). The trimer has the
CC following composition: FFI, FFF, FII, III. E.coli strains B and W,
CC which are known to contain only ArgI, produce only a trimer of
CC identical chains (III). {ECO:0000269|PubMed:4558857,
CC ECO:0000269|PubMed:789338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: ArgF might be the product of a relatively recent event
CC (duplication or transposition) peculiar to E.coli strain K-12.
CC {ECO:0000305|PubMed:4558857}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; X00759; CAA25329.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08694.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73376.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76057.1; -; Genomic_DNA.
DR PIR; A64753; OWECF.
DR RefSeq; NP_414807.1; NC_000913.3.
DR RefSeq; WP_001281825.1; NZ_LN832404.1.
DR AlphaFoldDB; P06960; -.
DR SMR; P06960; -.
DR BioGRID; 4261491; 11.
DR ComplexPortal; CPX-5625; Ornithine transcarbamoylase complex, argFII variant.
DR ComplexPortal; CPX-5626; Ornithine transcarbamoylase complex, argFFI variant.
DR ComplexPortal; CPX-5627; Ornithine transcarbamoylase complex, argFFF variant.
DR IntAct; P06960; 7.
DR STRING; 511145.b0273; -.
DR SWISS-2DPAGE; P06960; -.
DR PaxDb; P06960; -.
DR PRIDE; P06960; -.
DR EnsemblBacteria; AAC73376; AAC73376; b0273.
DR EnsemblBacteria; BAE76057; BAE76057; BAE76057.
DR GeneID; 944844; -.
DR KEGG; ecj:JW0266; -.
DR KEGG; eco:b0273; -.
DR PATRIC; fig|1411691.4.peg.2007; -.
DR EchoBASE; EB0065; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_6; -.
DR InParanoid; P06960; -.
DR OMA; NLSRWCD; -.
DR PhylomeDB; P06960; -.
DR BioCyc; EcoCyc:CHAINF-MON; -.
DR BioCyc; MetaCyc:CHAINF-MON; -.
DR SABIO-RK; P06960; -.
DR UniPathway; UPA00068; UER00112.
DR PRO; PR:P06960; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009348; C:ornithine carbamoyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IDA:EcoCyc.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0019240; P:citrulline biosynthetic process; IDA:ComplexPortal.
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 Direct protein sequencing; Metal-binding; Reference proteome; Transferase;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3968036"
FT CHAIN 2..334
FT /note="Ornithine carbamoyltransferase subunit F"
FT /id="PRO_0000112919"
FT BINDING 56..59
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 83
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 107
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 134..137
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 168
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 232
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 236..237
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 274..275
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 320
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT CONFLICT 121
FT /note="A -> P (in Ref. 1; CAA25329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36827 MW; C1EA07CD2AFC39C4 CRC64;
MSDLYKKHFL KLLDFTPAQF TSLLTLAAQL KADKKNGKEV QKLTGKNIAL IFEKDSTRTR
CSFEVAAFDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGHG QEVVETLAQY
AGVPVWNGLT NEFHPTQLLA DLMTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT
GLDLRLLAPK ACWPEESLVA ECSALAEKHG GKITLTEDVA AGVKGADFIY TDVWVSMGEA
KEKWAERIAL LRGYQVNAQM MALTDNPNVK FLHCLPAFHD DQTTLGKQMA KEFDLHGGME
VTDEVFESAA SIVFDQAENR MHTIKAVMMA TLGE
