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 01-MAY-2013, entry version 97.
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) (Campylobacter pylori 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;
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; SEFFEIV; -.
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:HAMAP.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA: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; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; FALSE_NEG.
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
//
