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Database: UniProt/TrEMBL
Entry: B5FSG3_SALDC
LinkDB: B5FSG3_SALDC
Original site: B5FSG3_SALDC 
ID   B5FSG3_SALDC            Unreviewed;       334 AA.
AC   B5FSG3;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   29-OCT-2014, entry version 51.
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=argF {ECO:0000313|EMBL:ACH75850.1};
GN   Synonyms=arcB {ECO:0000256|HAMAP-Rule:MF_01109};
GN   OrderedLocusNames=SeD_A4853 {ECO:0000313|EMBL:ACH75850.1};
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851 {ECO:0000313|EMBL:ACH75850.1, ECO:0000313|Proteomes:UP000008322};
RN   [1] {ECO:0000313|EMBL:ACH75850.1, ECO:0000313|Proteomes:UP000008322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853 {ECO:0000313|EMBL:ACH75850.1,
RC   ECO:0000313|Proteomes:UP000008322};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate
CC       + L-citrulline. {ECO:0000256|HAMAP-Rule:MF_01109,
CC       ECO:0000256|SAAS:SAAS00009104}.
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:SAAS00009106}.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|RuleBase:RU003634}.
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DR   EMBL; CP001144; ACH75850.1; -; Genomic_DNA.
DR   RefSeq; YP_002218334.1; NC_011205.1.
DR   ProteinModelPortal; B5FSG3; -.
DR   STRING; 439851.SeD_A4853; -.
DR   EnsemblBacteria; ACH75850; ACH75850; SeD_A4853.
DR   PATRIC; 18497745; VBISalEnt111443_4742.
DR   eggNOG; COG0078; -.
DR   HOGENOM; HOG000022686; -.
DR   OMA; YQRHFLR; -.
DR   OrthoDB; EOG690MGV; -.
DR   BioCyc; SENT439851:GH2Z-4795-MONOMER; -.
DR   UniPathway; UPA00254; UER00365.
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; Orn_carbamltrans.
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   Arginine metabolism {ECO:0000256|HAMAP-Rule:MF_01109};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008322};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|SAAS:SAAS00009103};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|RuleBase:RU003634}.
FT   REGION       56     60       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      273    276       Ornithine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     107    107       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     134    134       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   SITE         31     31       Important for structural integrity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   SITE        147    147       Important for structural integrity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
SQ   SEQUENCE   334 AA;  36742 MW;  E9130C76A2076EB4 CRC64;
     MSTFYQKPFL KLLDFTASEL TALLQLAAEL KADKKNGKEE QKLVGKNIAL IFEKDSTRTR
     CSFEVAAYDQ GARVTYLGSS GSQIGHKESI KDTARVLGRM FDGIQYRGYG QEIVETLAEY
     SGVPVWNGLT DEYHPTQLLA DLLTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT
     GLDLRLVAPK ACWPQAALVA ECSAMAKKNG GAITLTEDIA SGVKGADFIY TDVWVSMGEP
     KEKWAERIAL LRDYQVNSQM MALTGNPQVK FLHCLPAFHD DETTLGKKMA EEYGLHGGME
     VTDEVFESAA SIVFDEAENR MHTIKAVMVA TLSK
//
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