(data stored in SCRATCH zone)

SWISSPROT: D3VIS5_XENNA

ID   D3VIS5_XENNA            Unreviewed;       337 AA.
AC   D3VIS5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Ornithine carbamoyltransferase {ECO:0000256|SAAS:SAAS00393033};
DE            EC=2.1.3.3 {ECO:0000256|SAAS:SAAS00393033};
GN   Name=argI {ECO:0000313|EMBL:CBJ88625.1};
GN   OrderedLocusNames=XNC1_0551 {ECO:0000313|EMBL:CBJ88625.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88625.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88625.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group
CC       from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine
CC       (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00009102}.
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:0000256|HAMAP-
CC         Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
CC       ECO:0000256|SAAS:SAAS00341539}.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|RuleBase:RU003634,
CC       ECO:0000256|SAAS:SAAS00578869}.
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DR   EMBL; FN667742; CBJ88625.1; -; Genomic_DNA.
DR   RefSeq; WP_010845165.1; NC_014228.1.
DR   STRING; 406817.XNC1_0551; -.
DR   EnsemblBacteria; CBJ88625; CBJ88625; XNC1_0551.
DR   KEGG; xne:XNC1_0551; -.
DR   eggNOG; ENOG4105DBV; Bacteria.
DR   eggNOG; COG0078; LUCA.
DR   HOGENOM; HOG000022686; -.
DR   KO; K00611; -.
DR   OMA; QVNMDVV; -.
DR   Proteomes; UP000008075; 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   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;
DR   PRODOM; D3VIS5.
DR   SWISS-2DPAGE; D3VIS5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|SAAS:SAAS00420337};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|RuleBase:RU003634, ECO:0000256|SAAS:SAAS00470455,
KW   ECO:0000313|EMBL:CBJ88625.1}.
FT   DOMAIN        7    147       OTCace_N. {ECO:0000259|Pfam:PF02729}.
FT   DOMAIN      155    329       OTCace. {ECO:0000259|Pfam:PF00185}.
FT   REGION       56     59       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      134    137       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      235    236       Ornithine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   REGION      273    274       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   BINDING      83     83       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     107    107       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     167    167       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     231    231       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     319    319       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
SQ   SEQUENCE   337 AA;  37585 MW;  BE700F63803B46EE CRC64;
     MNPFFQRSIL RLLDITPIEI NTLLTLSHKL KANKKSGIES PLLTGKNIAL IFEKDSTRTR
     CAFEVAAHDQ GASVTYLGTH GSQIGHKESI KDTARVLGRL YDGLQYRGHG QHIVETMAQY
     AGVPVWNGLT DEFHPTQLLA DLLTIQEHSQ KSLSQIKFAY LGDARNNMGN TMLEAATLTG
     MDLRLIAPET CWPDVNLIAE CQKLAEKTGG QITLTEDIAQ GVKDADFLYT DVWVSMGEPK
     SVWQERIALL RSYQVNMGVI KLTGNPEVKF LHCLPAFHNE ETTLGKQLAE EFNLYGGLEV
     TNEVFESEHS IVFDQAENRM HTIKALMVAT MVENLVV
//

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