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Database: UniProt
Entry: O25577
LinkDB: O25577
Original site: O25577 
ID   CARB_HELPY              Reviewed;        1085 AA.
AC   O25577;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   13-FEB-2019, entry version 126.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000255|HAMAP-Rule:MF_01210};
GN   OrderedLocusNames=HP_0919;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter
OS   pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01210};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
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       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
DR   EMBL; AE000511; AAD07963.1; -; Genomic_DNA.
DR   PIR; G64634; G64634.
DR   RefSeq; NP_207711.1; NC_000915.1.
DR   RefSeq; WP_001126584.1; NC_018939.1.
DR   ProteinModelPortal; O25577; -.
DR   SMR; O25577; -.
DR   DIP; DIP-3181N; -.
DR   IntAct; O25577; 6.
DR   MINT; O25577; -.
DR   STRING; 85962.HP0919; -.
DR   PaxDb; O25577; -.
DR   PRIDE; O25577; -.
DR   EnsemblBacteria; AAD07963; AAD07963; HP_0919.
DR   GeneID; 899448; -.
DR   KEGG; heo:C694_04730; -.
DR   KEGG; hpy:HP0919; -.
DR   PATRIC; fig|85962.47.peg.984; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
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; IPR033937; MGS_CPS_CarB.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
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.
DR   PROSITE; PS51855; MGS; 1.
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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1085       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145010.
FT   DOMAIN      131    326       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      678    871       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      952   1085       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     157    214       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     704    764       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    399       Carboxyphosphate synthetic domain.
FT   REGION      400    552       Oligomerization domain.
FT   REGION      553    951       Carbamoyl phosphate synthetic domain.
FT   REGION      952   1085       Allosteric domain.
FT   METAL       283    283       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       297    297       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       297    297       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       830    830       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       842    842       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       842    842       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       844    844       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1085 AA;  120074 MW;  696E124A50DB34C1 CRC64;
     MPKRTDISNI LLIGSGPIVI GQACEFDYSG TQSCKTLKSL GYRVILINSN PATVMTDPEF
     SHQTYIQPIT PENIATIIEK EKIDAILPTM GGQTALNAVM QMHQKGMLEG VELLGAKIEA
     IKKGEDRQAF KEAMLKIGMD LPKGRYAYTE LEALEAINEI GFPAIIRASF TLAGGGSGVA
     YNIEEFQELA KNALDASPIN EILIEESLLG WKEYEMEVIR DSKDNCIIVC CIENIDPMGV
     HTGDSITIAP SLTLTDKEYQ RMRDASFAIL REIGVDTGGS NVQFAIHPET LRMVVIEMNP
     RVSRSSALAS KATGFPIAKV ATMLAVGFSL DEIQNDITNT PASFEPSLDY IVVKIPRFAF
     EKFAGVSSTL GTSMKSIGEV MAIGGNFLEA LQKALCSLEN NWLGFESLSK DLEAIKKEIR
     RPNPKRLLYI ADAFRLGVCV DEVFELCQID RWFLSQIQKL VEVEESINSS VLTDAKKLRG
     LKNLGFSDAR IAAKIKENEN LEVSPFEVEL ARSNLQIVPN FEEVDTCAAE FLSLTPYLYS
     TYAPNPLPPI ENKQEKKEKK ILIIGSGPNR IGQGIEFDYC CVHASLALKD LNIKSVMFNC
     NPETVSTDYD TSDTLYFEPI HFECVKSIIQ RERVDGIIVH FGGQTPLKLA KDLAKMQAPI
     IGTPFKVIDI AEDREKFSLF LKELDIKQPK NGMAKSVDEA YSIANVIGFP IIVRPSYVLG
     GQHMQILENI EELRHYLESV THALEISPKN PLLIDKFLEK AVELDVDAIC DKKEVYIAGI
     LQHIEEAGIH SGDSACFIPS TLSPEILDEI ERVSAKIALH LGVVGLLNIQ FAVHQNSLYL
     IEVNPRASRT VPFLSKALGV PLAKVATRVM VLEDLKEALK FYDKKNIVGY SKGVYKPKMP
     HFVALKEAVF PFNKLYGSDL ILGPEMKSTG EVMGIARSLG LAFFKAQTAC FNPIKNKGLI
     FVSIKDKDKE EACVLMKRLV QLGFELCATE GTHKALEKAG VKSLKVLKIS EGRPNIMDLM
     MNGEISMAIN TSDHKSQDDA KLIRASVLKN HVSYFTTLST IEVLLLALEE SSKEDELLAL
     QDYLK
//
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