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Database: UniProt
Entry: P46056
LinkDB: P46056
Original site: P46056 
ID   CARB_TRICU              Reviewed;        1176 AA.
AC   P46056;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   05-DEC-2018, entry version 101.
DE   RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, ammonia chain;
GN   Name=argA;
OS   Trichosporon cutaneum (Yeast) (Oidium cutaneum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Trichosporonales; Trichosporonaceae;
OC   Cutaneotrichosporon.
OX   NCBI_TaxID=5554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 70698;
RX   PubMed=8188603; DOI=10.1128/jb.176.10.3021-3032.1994;
RA   Reiser J., Glumoff V., Ochsner U.A., Fiechter A.;
RT   "Molecular analysis of the Trichosporon cutaneum DSM 70698 argA gene
RT   and its use for DNA-mediated transformations.";
RL   J. Bacteriol. 176:3021-3032(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: In eukaryotes this enzyme is synthesized by two
CC       pathway-specific (arginine and pyrimidine) under separate control.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
DR   EMBL; L08965; AAA21443.1; -; Genomic_DNA.
DR   ProteinModelPortal; P46056; -.
DR   SMR; P46056; -.
DR   PRIDE; P46056; -.
DR   UniPathway; UPA00068; UER00171.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Cytoplasm; Ligase; Manganese; Metal-binding; Nucleotide-binding;
KW   Repeat.
FT   CHAIN         1   1176       Carbamoyl-phosphate synthase arginine-
FT                                specific large chain.
FT                                /FTId=PRO_0000145090.
FT   DOMAIN      201    391       ATP-grasp 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      734    931       ATP-grasp 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      999   1154       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     221    275       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     366    416       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       348    348       Manganese 1. {ECO:0000250}.
FT   METAL       362    362       Manganese 1. {ECO:0000250}.
FT   METAL       362    362       Manganese 2. {ECO:0000250}.
FT   METAL       364    364       Manganese 2. {ECO:0000250}.
FT   METAL       884    884       Manganese 3. {ECO:0000250}.
FT   METAL       902    902       Manganese 3. {ECO:0000250}.
SQ   SEQUENCE   1176 AA;  128910 MW;  89D74088B9AA6AA8 CRC64;
     MLRSISIASR AAGPVRPVAR ARTAVGVVAP PRVCCCAPAV GNYGQVDGKA TLNSLRRLPA
     GYRPRSCPSS RSPDVKKVLV VGSGGLSIGQ AGEFDYSGSQ AIKALRESNI ETILINPNIA
     TIQTSHHLAS EIYFLPVTAD YVAYVLEKER PDGILLTFGG QSALNVGIQL EKMGVLERLG
     VQVLGTPIRT LEISEDRDLF VQALNEIDIP AAQSTAVSTI QDALDAAKTI GYPIILRSAF
     SLGGLGSFPH DEEELRNLAA KSLSLSPQVL IEKSLKGWKE VEYEVVRDAA DNTIICCNME
     NFDPLGTHTG DSIVVAPSQT LTDEYHMLRS AAIKIVRHVG VVGECNVQYA LDPNSRDYRV
     IEMNARLSRS SALASKATGY PLAYTAAKIA LGHTLRELPN AVTKSTTACF EPSLDYIVTK
     IPKWDLAKFQ HVERNVGSAM KSVGEVMAIG RTFEESLQKA IRQVDPNFAG FEAYWKPEDM
     ITALTNNNDR RLFAIAHAML NLDYSVDYLH DLTKIDKWFL YKLENIVAVH KQLRSTPFEQ
     LDKELVMTAK KTGFSDLQIA QLTGKTEAEV RTLRKQFGVT PFVKRIDTLA AEFPAYTNYL
     YTSYNATTHD VKFDNGTMVL GSGVYRIGSS VEFDWCAVTC SRAIRDLGKK TIMINYNPET
     VSTDFDEADR LYFEELGFER VMDIYDLEGA SGVVVSVGGQ LPQNIALRLK KAGVQVLGTD
     PEMIDSAEDR HKFSSILDSI GVDQPAWTEA SSLASAKEFA NRVGYPVLIR PSYVLSGAAM
     NVVWDEAQLE HNLTLATNVS PDHPVVISQF IDNAQEIDVD AVAHKGKLLV HAVSEHVENA
     GVHSGDATLV LPPFSVNQHD LGRLKTIAEK VAQAFQISGP FNMQIIRKPP TGEEDAELKV
     IECNLRASRS FPFVSKVLGH NFIDTASAAI MDTNVPAPID LMAQKRDYVA IKVPQFSWTR
     LPGADPFLGV EMASTGEVAS FGKDIYDAYW AALLSVNGMK LPKANSGILL GGDITRPEMT
     EVAKNLINLG FSLYTYDPKV EAHINDQPYL SIKKILVPVK DKKKLREILE EHEIQTVINM
     ARSRAATTLD EDYAARRAAV DFGIPLINNP KLAVLFTETL EKKFVKNNPI PYSEGFKPSE
     VGSWRDFVGE AATTKLEGIA WTGEAYCIIL IPGIGV
//
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