(data stored in ACNUC7421 zone)

SWISSPROT: C3MFB7_SINFN

ID   C3MFB7_SINFN            Unreviewed;       305 AA.
AC   C3MFB7;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 64.
DE   RecName: Full=Ornithine carbamoyltransferase, catabolic {ECO:0000256|HAMAP-Rule:MF_01109};
DE            Short=OTCase {ECO:0000256|HAMAP-Rule:MF_01109};
DE            EC=2.1.3.3 {ECO:0000256|HAMAP-Rule:MF_01109};
GN   Name=arcB {ECO:0000256|HAMAP-Rule:MF_01109};
GN   Synonyms=argF {ECO:0000313|EMBL:ACP23954.1};
GN   OrderedLocusNames=NGR_c01520 {ECO:0000313|EMBL:ACP23954.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23954.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23954.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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: Carbamoyl phosphate + L-ornithine = phosphate
CC       + L-citrulline. {ECO:0000256|HAMAP-Rule:MF_01109,
CC       ECO:0000256|SAAS:SAAS00106053}.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01109}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
CC       ECO:0000256|SAAS:SAAS00106153}.
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; CP001389; ACP23954.1; -; Genomic_DNA.
DR   RefSeq; WP_012706739.1; NC_012587.1.
DR   RefSeq; YP_002824707.1; NC_012587.1.
DR   ProteinModelPortal; C3MFB7; -.
DR   STRING; 394.NGR_c01520; -.
DR   EnsemblBacteria; ACP23954; ACP23954; NGR_c01520.
DR   GeneID; 7790731; -.
DR   KEGG; rhi:NGR_c01520; -.
DR   PATRIC; fig|394.7.peg.2947; -.
DR   eggNOG; ENOG4105DBV; Bacteria.
DR   eggNOG; COG0078; LUCA.
DR   HOGENOM; HOG000022686; -.
DR   KO; K00611; -.
DR   OMA; HPMFLGK; -.
DR   OrthoDB; POG091H0543; -.
DR   UniPathway; UPA00254; UER00365.
DR   Proteomes; UP000001054; 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-HAMAP.
DR   GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019546; P:arginine deiminase pathway; IEA:UniProtKB-HAMAP.
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; 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; C3MFB7.
DR   SWISS-2DPAGE; C3MFB7.
KW   Arginine metabolism {ECO:0000256|HAMAP-Rule:MF_01109};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|SAAS:SAAS00009103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|RuleBase:RU003634, ECO:0000256|SAAS:SAAS00106165,
KW   ECO:0000313|EMBL:ACP23954.1}.
FT   DOMAIN        5    145       OTCace_N. {ECO:0000259|Pfam:PF02729}.
FT   DOMAIN      151    300       OTCace. {ECO:0000259|Pfam:PF00185}.
FT   REGION       54     57       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      132    135       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      227    228       Ornithine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   REGION      262    263       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   BINDING      81     81       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     105    105       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     163    163       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     223    223       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     290    290       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
SQ   SEQUENCE   305 AA;  33537 MW;  4681458A0AFA1276 CRC64;
     MTATRHFLDL SAMTGADLRT IIDDARVRKT ATKAGTAEKP LAGKMLAMIF EKPSTRTRVS
     FDVGMRQLGG ETLFLSGTEM QLGRAETIGD TAKVLSRYVD AIMIRTTDHR RLLELAEHAT
     VPVINGLTDD THPCQIMADI MTFEEHRGPV QGKTIAWTGD GNNVLHSLIE GSARFGYRMN
     MAVPLGSEPQ DKFLNWARNN GGEILLCHEA EQAVAGAHCV VTDTWVSMNQ EHRARGHNVF
     QPYQVNAALM KHAVPEAVFM HCLPAHRGEE VTDEVIDGPQ SVVFDAAENR LHAQKSILAW
     CLGAV
//

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