OTC_THEMA
ID OTC_THEMA Reviewed; 313 AA.
AC P96108;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01109};
DE Short=OTCase {ECO:0000255|HAMAP-Rule:MF_01109};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=argF {ECO:0000255|HAMAP-Rule:MF_01109}; OrderedLocusNames=TM_1097;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RA van de Casteele M., Legrain C., Glansdorff N.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of ornithine carbamoyltransferase (TM1097) from
RT Thermotoga maritima at 2.25 a resolution.";
RL Submitted (AUG-2004) to the PDB data bank.
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:0000255|HAMAP-Rule:MF_01109}.
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 -!- 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:0000255|HAMAP-Rule:MF_01109}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000255|HAMAP-Rule:MF_01109}.
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DR EMBL; Y10661; CAA71670.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36173.1; -; Genomic_DNA.
DR PIR; C72294; C72294.
DR RefSeq; NP_228903.1; NC_000853.1.
DR RefSeq; WP_004080343.1; NZ_CP011107.1.
DR PDB; 1VLV; X-ray; 2.25 A; A=1-313.
DR PDBsum; 1VLV; -.
DR AlphaFoldDB; P96108; -.
DR SMR; P96108; -.
DR STRING; 243274.THEMA_08860; -.
DR EnsemblBacteria; AAD36173; AAD36173; TM_1097.
DR KEGG; tma:TM1097; -.
DR eggNOG; COG0078; Bacteria.
DR InParanoid; P96108; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 988597at2; -.
DR UniPathway; UPA00068; UER00112.
DR EvolutionaryTrace; P96108; -.
DR Proteomes; UP000008183; 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; IBA:GO_Central.
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..313
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000113049"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 167
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 231
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 235..236
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 272..273
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 300
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000305|Ref.3"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 18..37
FT /evidence="ECO:0007829|PDB:1VLV"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1VLV"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1VLV"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:1VLV"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1VLV"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:1VLV"
FT HELIX 293..312
FT /evidence="ECO:0007829|PDB:1VLV"
SQ SEQUENCE 313 AA; 35362 MW; 0C813CAC3B8C6F8D CRC64;
MSVNLKGRSL LTLLDFSPEE IRYLLDISKQ VKMENRSKLR TERFKGMTLA MIFEKRSTRT
RLAFETAFAE EGGHPIFLSP NDIHLGAKES LEDTARVLGR MVDAIMFRGY KQETVEKLAE
YSGVPVYNGL TDEFHPTQAL ADLMTIEENF GRLKGVKVVF MGDTRNNVAT SLMIACAKMG
MNFVACGPEE LKPRSDVFKR CQEIVKETDG SVSFTSNLEE ALAGADVVYT DVWASMGEED
KEKERMALLK PYQVNERVME MTGKSETIFM HCLPAVKGQE VTYEVIEGKQ SRVWDEAENR
KHTIKAVMIA TLL
