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OTC_RHIME
ID   OTC_RHIME               Reviewed;         303 AA.
AC   Q92S99;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=argF; OrderedLocusNames=R00518; ORFNames=SMc02137;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
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DR   EMBL; AL591688; CAC45090.1; -; Genomic_DNA.
DR   RefSeq; NP_384624.1; NC_003047.1.
DR   RefSeq; WP_010968637.1; NC_003047.1.
DR   AlphaFoldDB; Q92S99; -.
DR   SMR; Q92S99; -.
DR   STRING; 266834.SMc02137; -.
DR   EnsemblBacteria; CAC45090; CAC45090; SMc02137.
DR   GeneID; 61601991; -.
DR   KEGG; sme:SMc02137; -.
DR   PATRIC; fig|266834.11.peg.1891; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_2_5; -.
DR   OMA; DGNNVCN; -.
DR   UniPathway; UPA00068; UER00112.
DR   Proteomes; UP000001976; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Reference proteome; Transferase.
FT   CHAIN           1..303
FT                   /note="Ornithine carbamoyltransferase"
FT                   /id="PRO_0000112998"
FT   BINDING         52..55
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         79
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         103
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         130..133
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         161
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..261
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         288
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   303 AA;  33436 MW;  1E9B2C5B94B2D2DA CRC64;
     MTRHFLDLSA MTATDLRTII DDARVRKSAT KAGTAEKPLA GKMLAMIFEK PSTRTRVSFD
     VGMRQLGGET LFLSGTEMQL GRAETIGDTA KVLSRYVDAI MIRTTDHRRL LEMAEHATVP
     VINGLTDDTH PCQIMADILT FEEHRGPVKG KTIAWTGDGN NVLHSLIEGS ARFGYRMNMA
     VPLGSEPHDK FLNWARNNGA EVLLSHEAEQ AVAGAHCVVT DTWISMNQEH RARGHNVFQP
     YQVNGALMKH AAPDALFMHC LPAHRGEEVT DEVIDGPQSV VFDEAENRLH AQKSILAWCM
     GAV
 
 
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