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CARB_CAMJE
ID   CARB_CAMJE              Reviewed;        1089 AA.
AC   Q9PIL7; Q0PBM7;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
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}; OrderedLocusNames=Cj0279;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC       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 the
CC       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}.
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DR   EMBL; AL111168; CAL34432.1; -; Genomic_DNA.
DR   PIR; E81446; E81446.
DR   RefSeq; WP_002858661.1; NC_002163.1.
DR   RefSeq; YP_002343720.1; NC_002163.1.
DR   AlphaFoldDB; Q9PIL7; -.
DR   SMR; Q9PIL7; -.
DR   STRING; 192222.Cj0279; -.
DR   PaxDb; Q9PIL7; -.
DR   PRIDE; Q9PIL7; -.
DR   EnsemblBacteria; CAL34432; CAL34432; Cj0279.
DR   GeneID; 904603; -.
DR   KEGG; cje:Cj0279; -.
DR   PATRIC; fig|192222.6.peg.272; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_7; -.
DR   OMA; IEPAGIH; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000799; Chromosome.
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   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; 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; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome; Repeat.
FT   CHAIN           1..1089
FT                   /note="Carbamoyl-phosphate synthase large chain"
FT                   /id="PRO_0000144998"
FT   DOMAIN          131..326
FT                   /note="ATP-grasp 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          680..871
FT                   /note="ATP-grasp 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          952..1089
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   REGION          1..399
FT                   /note="Carboxyphosphate synthetic domain"
FT   REGION          400..553
FT                   /note="Oligomerization domain"
FT   REGION          554..951
FT                   /note="Carbamoyl phosphate synthetic domain"
FT   REGION          952..1089
FT                   /note="Allosteric domain"
FT   BINDING         157..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         707..763
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         830
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         842
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         842
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         844
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1089 AA;  120941 MW;  F2B051B8B523E7EC CRC64;
     MPKRTDIKSI LLIGSGPIVI GQACEFDYSG TQAAKTLKEL GYRVVLINSN PATIMTDPEF
     ADATYIEPIT KESILSIIKK EKIDAILPTM GGQVALNVAM EVYESGLLGD VKFLGANPEA
     IKKGEDRQVF KECMKKIGMD LPKSMYAYNY DEALKAVDEI DFPLMIRASY TLGGAGSGVV
     YNMDEFKELT NTALALSPIH EILIEESLLG WKEYEMEVIR DRADNCIIVC SIENIDPMGV
     HTGDSITIAP ALTLTDKEYQ VMRNASFAIL REIGVDTGGS NVQFAINPKN GRMIVIEMNP
     RVSRSSALAS KATGYPIAKV ATLLAVGFSL DEIKNDITGT PASFEPVIDY IVTKIPRFTF
     EKFPGANTTL GTAMKSVGEV MAIGRTFKES IQKALCSLER SLSGFDRVKF EDRNDLVFKI
     RNANEKRLLY VAQAFREGFS VEELYELCKI DPWFLTQIKE IVDFEEQIDM DILNNKALLR
     KAKTMGFSDK MIALLVNLKD NLELSQNDIY YVRMKQKIIA EFSEVDTCAG EFEALTPYLY
     SSINVSELTQ SKNDAKDKKE KKVMIIGGGP NRIGQGIEFD YACVHASFAL KDMGIKTIMY
     NCNPETVSTD YDTSDILYFE PIDFEHLRAV IEREKPDGVI VHFGGQTPLK FAKRLSAFGA
     KIIGTSARVI DMAEDRKKFA EFITKLGINQ PKNSTATSVE EAVLKASDIG YPVLVRPSYV
     LGGRAMRVVN DEAELRLYMQ EAVDVSDKSP VLIDQFLDNA TEIDVDAICD GKDVYVAGIM
     EHIEEAGIHS GDSACSLPPC NIDEKMQEFI AQKTADIALN LGVVGLLNIQ FALHNNELYM
     IEVNPRASRT IPFVSKATGI PLAKVATRVM WQGNLKEALK FYDTFKVVNF DTKILRPKTP
     KYMSVKEAVF PFAKLSGSDL ELGPEMRSTG EVMGISKDFA NSYAKSQIAS FNHLPEQGVV
     FISLKDKDKK YTKKIAAEYV KLGFKLMATG GTCKEILESG FECELVHKIS EGRPNVEDKL
     KNGEIHLVIN TSDSHSFKGD TKKIRENIIR FKIPYFTNLR SALAGAKSIK AIQSKSCLDV
     KSLQEWLKS
 
 
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