OTC_MYCTU
ID OTC_MYCTU Reviewed; 307 AA.
AC P9WIT9; L0T7B5; P0A5M8; P94991; Q02095;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000303|PubMed:18062991};
DE Short=OTCase {ECO:0000303|PubMed:18062991};
DE EC=2.1.3.3 {ECO:0000305|PubMed:18062991};
GN Name=argF {ECO:0000255|HAMAP-Rule:MF_01109}; OrderedLocusNames=Rv1656;
GN ORFNames=MTCY06H11.21;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP SUBUNIT.
RX PubMed=17012791; DOI=10.1107/s1744309106034609;
RA Moradian F., Garen C., Cherney L., Cherney M., James M.N.;
RT "Expression, purification, crystallization and preliminary X-ray analysis
RT of two arginine-biosynthetic enzymes from Mycobacterium tuberculosis.";
RL Acta Crystallogr. F 62:986-988(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-307 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REACTION
RP MECHANISM, AND SUBUNIT.
RX PubMed=18062991; DOI=10.1016/j.jmb.2007.11.025;
RA Sankaranarayanan R., Cherney M.M., Cherney L.T., Garen C.R., Moradian F.,
RA James M.N.;
RT "The crystal structures of ornithine carbamoyltransferase from
RT Mycobacterium tuberculosis and its ternary complex with carbamoyl phosphate
RT and L-norvaline reveal the enzyme's catalytic mechanism.";
RL J. Mol. Biol. 375:1052-1063(2008).
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:0000305|PubMed:18062991}.
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:0000305|PubMed:18062991};
CC -!- ACTIVITY REGULATION: Competitively inhibited by L-norvaline (NVA).
CC {ECO:0000269|PubMed:18062991}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000305}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17012791,
CC ECO:0000269|PubMed:18062991}.
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; AL123456; CCP44421.1; -; Genomic_DNA.
DR PIR; C70621; C70621.
DR RefSeq; NP_216172.1; NC_000962.3.
DR RefSeq; WP_003408165.1; NZ_NVQJ01000069.1.
DR PDB; 2I6U; X-ray; 2.20 A; A/B/C=2-307.
DR PDB; 2P2G; X-ray; 2.70 A; A/B/C/D/E/F=2-307.
DR PDB; 7NNF; X-ray; 1.52 A; A/B/C/D/E/F=2-307.
DR PDB; 7NNV; X-ray; 1.67 A; A/B/C/D/E/F=2-307.
DR PDB; 7NNW; X-ray; 1.78 A; A/B/C/D/E/F=2-307.
DR PDB; 7NNY; X-ray; 1.57 A; A/B/C/D/E/F=2-307.
DR PDB; 7NNZ; X-ray; 1.68 A; A/B/C/D/E/F=2-307.
DR PDB; 7NOR; X-ray; 1.59 A; A/B/C/D/E/F=2-307.
DR PDB; 7NOS; X-ray; 1.77 A; A/B/C/D/E/F=2-307.
DR PDB; 7NOU; X-ray; 1.98 A; A/B/C/D/E/F=2-307.
DR PDB; 7NOV; X-ray; 1.90 A; A/B/C/D/E/F=2-307.
DR PDB; 7NP0; X-ray; 1.76 A; A/B/C/D/E/F=2-307.
DR PDBsum; 2I6U; -.
DR PDBsum; 2P2G; -.
DR PDBsum; 7NNF; -.
DR PDBsum; 7NNV; -.
DR PDBsum; 7NNW; -.
DR PDBsum; 7NNY; -.
DR PDBsum; 7NNZ; -.
DR PDBsum; 7NOR; -.
DR PDBsum; 7NOS; -.
DR PDBsum; 7NOU; -.
DR PDBsum; 7NOV; -.
DR PDBsum; 7NP0; -.
DR AlphaFoldDB; P9WIT9; -.
DR SMR; P9WIT9; -.
DR STRING; 83332.Rv1656; -.
DR PaxDb; P9WIT9; -.
DR GeneID; 885462; -.
DR KEGG; mtu:Rv1656; -.
DR TubercuList; Rv1656; -.
DR eggNOG; COG0078; Bacteria.
DR OMA; DGNNVCN; -.
DR PhylomeDB; P9WIT9; -.
DR BRENDA; 2.1.3.3; 3445.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000001584; 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; IDA:MTBBASE.
DR GO; GO:0006526; P:arginine biosynthetic process; IMP:MTBBASE.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
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 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000112955"
FT BINDING 50..53
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT BINDING 77
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT BINDING 101
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT BINDING 128..131
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT BINDING 160
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT BINDING 224
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT BINDING 228..229
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT BINDING 264..265
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT BINDING 292
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:18062991,
FT ECO:0007744|PDB:2I6U"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:7NNF"
FT TURN 35..39
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:7NOR"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:7NNY"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:7NNY"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:7NNF"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:7NNF"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:7NNF"
FT HELIX 285..306
FT /evidence="ECO:0007829|PDB:7NNF"
SQ SEQUENCE 307 AA; 33057 MW; 7DC982EE07357F7E CRC64;
MIRHFLRDDD LSPAEQAEVL ELAAELKKDP VSRRPLQGPR GVAVIFDKNS TRTRFSFELG
IAQLGGHAVV VDSGSTQLGR DETLQDTAKV LSRYVDAIVW RTFGQERLDA MASVATVPVI
NALSDEFHPC QVLADLQTIA ERKGALRGLR LSYFGDGANN MAHSLLLGGV TAGIHVTVAA
PEGFLPDPSV RAAAERRAQD TGASVTVTAD AHAAAAGADV LVTDTWTSMG QENDGLDRVK
PFRPFQLNSR LLALADSDAI VLHCLPAHRG DEITDAVMDG PASAVWDEAE NRLHAQKALL
VWLLERS
