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Database: UniProt
Entry: Q9ZKT2
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ID   CARB_HELPJ              Reviewed;        1085 AA.
AC   Q9ZKT2;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   19-FEB-2014, entry version 101.
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=jhp_0853;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori
OS   J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G.,
RA   Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C.,
RA   Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F.,
RA   Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human
RT   gastric pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD06431.1; -; Genomic_DNA.
DR   PIR; H71880; H71880.
DR   RefSeq; NP_223571.1; NC_000921.1.
DR   ProteinModelPortal; Q9ZKT2; -.
DR   STRING; 85963.jhp0853; -.
DR   PRIDE; Q9ZKT2; -.
DR   EnsemblBacteria; AAD06431; AAD06431; jhp_0853.
DR   GeneID; 890029; -.
DR   KEGG; hpj:jhp0853; -.
DR   PATRIC; 20606457; VBIHelPyl98156_0931.
DR   eggNOG; COG0458; -.
DR   KO; K01955; -.
DR   OMA; RLVVIEM; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   ProtClustDB; PRK05294; -.
DR   BioCyc; HPYL85963:GJB9-868-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_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; 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   1085       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145011.
FT   DOMAIN      131    326       ATP-grasp 1.
FT   DOMAIN      678    871       ATP-grasp 2.
FT   NP_BIND     157    214       ATP (By similarity).
FT   NP_BIND     704    764       ATP (By similarity).
FT   REGION        1    399       Carboxyphosphate synthetic domain.
FT   REGION      400    551       Oligomerization domain.
FT   REGION      552    951       Carbamoyl phosphate synthetic domain.
FT   REGION      952   1085       Allosteric domain.
FT   METAL       283    283       Magnesium or manganese 1 (By similarity).
FT   METAL       297    297       Magnesium or manganese 1 (By similarity).
FT   METAL       297    297       Magnesium or manganese 2 (By similarity).
FT   METAL       299    299       Magnesium or manganese 2 (By similarity).
FT   METAL       830    830       Magnesium or manganese 3 (By similarity).
FT   METAL       842    842       Magnesium or manganese 3 (By similarity).
FT   METAL       842    842       Magnesium or manganese 4 (By similarity).
FT   METAL       844    844       Magnesium or manganese 4 (By similarity).
SQ   SEQUENCE   1085 AA;  119966 MW;  36DEFD313BE5C387 CRC64;
     MPKRTDISNI LLIGSGPIVI GQACEFDYSG TQSCKTLKSL GYRVILINSN PATVMTDPEF
     SHQTYIQPIT PENIAAIIKK EKIDAILPTM GGQTALNAVM QMHQRGMLEG VELLGAKIEA
     IKKGEDRQAF KEAMLKIGMD LPKGRYAYSE LEALEAISEI GFPAIIRASF TLAGGGSGVA
     YNIEEFQELA KNALDASPIN EILIEESLLG WKEYEMEVIR DGKDNCIIVC CIENIDPMGV
     HTGDSITIAP SLTLTDKEYQ RMRDASFAIL REIGVDTGGS NVQFAIHPET LRMVVIEMNP
     RVSRSSALAS KATGFPIAKV ATMLAVGFSL DEIKNDITNT PASFEPSLDY IVVKIPRFAF
     EKFAGVSSTL GTSMKSIGEV MAIGGNFLEA LQKALCSLEN NWLGFESLSK DLEAIKKEIR
     RPNPKRLLYI ADAFRLGVSV DEVFELCQID RWFLSQIQKL VKAEEGINSS VLTDAKKLRG
     LKNLGFSDAR IATKIKENEN LEVSPFEVEL ARSNLQIAPH FEEVDTCAAE FLSLTPYLYS
     TYAPNPLPPI GNKQEKQEKK ILIIGSGPNR IGQGIEFDYC CVHASFALKD LNIKSVMLNC
     NPETVSTDYD TSDTLYFEPI HFECVKSIIQ RERVDGIIVH FGGQTPLKLA KDLAKMQAPI
     IGTPFKVIDI AEDREKFSLF LKELDIKQPE NGMAKSVDEA YSIANAIGFP IIVRPSYVLG
     GQHMQILENI EELRHYLESV THSLEISPKN PLLIDKFLEK AVELDVDAIC DKKEVYIAGI
     LQHIEEAGIH SGDSACFIPS TLSPEILDEI ERVSAKIALH LGVVGLLNIQ FAVYQNSLYL
     IEVNPRASRT VPFLSKALGV PLAKVATRVM VLEDLKEALK FYDKKNIVEY SKGVYKPKMP
     HFVALKEAVF PFNKLYGSDL ILGPEMKSTG EVMGIARSLG LAFFKAQTAC FNPIKNKGLI
     FVSIKDKDKE EACVLMKRLV ELGFELCTTE GTHKALEKAG VKSLKVLKIS EGRPNIMDLM
     MNGEISMAIN TSDHKSQDDA KLIRASVLKN HVSYFTTLSA IEVLLLALEE SSQEDELLAL
     QDYLK
//
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