CARB_CUTCT
ID CARB_CUTCT Reviewed; 1176 AA.
AC P46056;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Cutaneotrichosporon cutaneum (Yeast) (Trichosporon cutaneum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; 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 and
RT 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; carbamoyl
CC 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 the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: In eukaryotes this enzyme is synthesized by two pathway-
CC specific (arginine and pyrimidine) under separate control.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; L08965; AAA21443.1; -; Genomic_DNA.
DR AlphaFoldDB; P46056; -.
DR SMR; 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; IPR011607; MGS-like_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; Cytoplasm;
KW Ligase; Manganese; Metal-binding; Nucleotide-binding; Repeat.
FT CHAIN 1..1176
FT /note="Carbamoyl-phosphate synthase arginine-specific large
FT chain"
FT /id="PRO_0000145090"
FT DOMAIN 201..391
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 734..931
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 999..1154
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT BINDING 221..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 366..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 884
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 902
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="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
