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Database: UniProt
Entry: Q7VP67
LinkDB: Q7VP67
Original site: Q7VP67 
ID   CARB_HAEDU              Reviewed;        1075 AA.
AC   Q7VP67;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   19-FEB-2014, entry version 81.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN   Name=carB; OrderedLocusNames=HD_0233;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R.,
RA   Johnson L., Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CarB family.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains.
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DR   EMBL; AE017143; AAP95220.1; -; Genomic_DNA.
DR   RefSeq; NP_872831.1; NC_002940.2.
DR   ProteinModelPortal; Q7VP67; -.
DR   STRING; 233412.HD0233; -.
DR   PRIDE; Q7VP67; -.
DR   EnsemblBacteria; AAP95220; AAP95220; HD_0233.
DR   GeneID; 1490238; -.
DR   KEGG; hdu:HD0233; -.
DR   PATRIC; 20177039; VBIHaeDuc133973_0187.
DR   eggNOG; COG0458; -.
DR   KO; K01955; -.
DR   OMA; RLVVIEM; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   ProtClustDB; PRK05294; -.
DR   BioCyc; HDUC233412:GH5F-216-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 2.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
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; IPR016185; PreATP-grasp_dom.
DR   Pfam; PF00289; CPSase_L_chain; 2.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM00851; MGS; 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; 1.
DR   PROSITE; PS00867; CPSASE_2; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT   CHAIN         1   1075       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145008.
FT   DOMAIN      133    328       ATP-grasp 1.
FT   DOMAIN      673    864       ATP-grasp 2.
FT   NP_BIND     159    216       ATP (By similarity).
FT   NP_BIND     699    756       ATP (By similarity).
FT   REGION        1    403       Carboxyphosphate synthetic domain.
FT   REGION      404    548       Oligomerization domain.
FT   REGION      549    930       Carbamoyl phosphate synthetic domain.
FT   REGION      931   1075       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1 (By similarity).
FT   METAL       299    299       Magnesium or manganese 1 (By similarity).
FT   METAL       299    299       Magnesium or manganese 2 (By similarity).
FT   METAL       301    301       Magnesium or manganese 2 (By similarity).
FT   METAL       823    823       Magnesium or manganese 3 (By similarity).
FT   METAL       835    835       Magnesium or manganese 3 (By similarity).
FT   METAL       835    835       Magnesium or manganese 4 (By similarity).
FT   METAL       837    837       Magnesium or manganese 4 (By similarity).
SQ   SEQUENCE   1075 AA;  118332 MW;  67CAA6505FCA7A21 CRC64;
     MPKRTDINTI LIIGAGPIII GQACEFDYSG AQAVKALREE GYKVILVNSN PATIMTDPDM
     ADVTYIEPIQ WQTLEKIIEK ERPDAILPTM GGQTALNCAL ALSKNGVLKK YGVELIGATE
     DAIDKAEDRG RFKDAMTKIG LNTPKSFICH SFEEAWQAQE QVGFPTLIRP SFTMGGSGGG
     IAYNRDEFQA ICERGFEASP THELLIEQSV LGWKEYEMEV VRDKADNCII VCSIENFDPM
     GVHTGDSITV APAQTLTDKE YQIMRNASLA VLREIGVDTG GSNVQFAINP ANGEMIVIEM
     NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLNELRNDIT GGLIPTSFEP TIDYVVTKVP
     RFAFEKFPQA DDRLTTQMKS VGEVMAMGRT FQESLQKALR GLEIGICGFN LRSESPETIR
     RELANPGPNR ILYVADAFGA GFSLEEVHHY SKIDPWFLIQ IQDLVQEEMA LEKRAFTELD
     YAELRRLKRK GFSDKRIAQL IKVSESDVRA KRYALNLHPV YKRVDTCAGE FKADTAYLYS
     TYEDECEAKP TTRQKVMILG GGPNRIGQGI EFDYCCVHAA LALREAGFET IMVNCNPETV
     STDFDTSDRL YFEPLTLEDV LEIIYKEQPW GVIVHYGGQT PLKLAHALEQ NGVNIIGTSA
     DSIDAAEDRA RFQKILTDLG LKQPNNRTAR NAEEAVKLAE EVGYPLVVRP SYVLGGRAMQ
     IVYNVDELNN YMQEAVSVSN DSPILLDHFL KNAIEVDVDC ICDSEQVLIG GIMQHVEQAG
     IHSGDSACSL PAYSLTNEVQ GEIRRQTSAM AFALGVKGLM NVQFAVQNET IYVLEVNPRA
     SRTVPFVSKA TGNPLAKIAA LVMAGKSLAE QNATTEIIPP YFSVKEAVFP FIKFPGVDTT
     LSPEMRSTGE VMGTGQSFAE AYYKAQLGAG ERIPSTGKVF LSIADEDKPQ IIRVAQYLQA
     EGYGLCATIG TAQYLRENGV GVQIINKVRE GRPNIVDSIK NNEIAMIINT VNNLPESIKE
     AQEIRRNALK LHIPTYTTLA AAEAISEAVR HINKYDVNAL QQLHLSSALA NQITR
//
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