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Database: UniProt
Entry: A5D508
LinkDB: A5D508
Original site: A5D508 
ID   CARB_PELTS              Reviewed;        1083 AA.
AC   A5D508;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JAN-2019, entry version 83.
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=PTH_0505;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-
RT   associated evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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; AP009389; BAF58686.1; -; Genomic_DNA.
DR   ProteinModelPortal; A5D508; -.
DR   SMR; A5D508; -.
DR   STRING; 370438.PTH_0505; -.
DR   PRIDE; A5D508; -.
DR   EnsemblBacteria; BAF58686; BAF58686; PTH_0505.
DR   KEGG; pth:PTH_0505; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; HERFFAI; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000006556; 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_A; CPSase_L_chain_A; 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;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1083       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000085560.
FT   DOMAIN      133    327       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      673    863       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      932   1069       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     699    756       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    401       Carboxyphosphate synthetic domain.
FT   REGION      402    548       Oligomerization domain.
FT   REGION      549    931       Carbamoyl phosphate synthetic domain.
FT   REGION      932   1083       Allosteric domain.
FT   METAL       284    284       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       298    298       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       298    298       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       300    300       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       822    822       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       834    834       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       834    834       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       836    836       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1083 AA;  116854 MW;  E5A4BD6F2DD9F8D3 CRC64;
     MPRRKDIRKV LVIGSGPIII GQAAEFDYAG TQACKALREE GVSVVLVNSN PATIMTDLDI
     ADQVYIEPLA WDSVAEIIAR ERPDGLLPTL GGQTGLNIAV ELSEKGVLQD YGVELLGTPL
     ESIKKAENRE LFKNLMLEIG EPVPRSTIAG SVEECLAFAG EIGYPVIVRP AYTLGGTGGG
     IACREQELVE IAGRGLKMSM IGQVLLEQSV AGWKEIEYEV MRDGADNCIT VCNMENVDPV
     GIHTGDSIVV APSQTLSDKE YQLLRSAALR IIRALKVEGG CNVQFALDLN SMAYYVIEVN
     PRVSRSSALA SKATGYPIAK VAAKIAVGLT LDEIKNPVTG KTYACFEPAL DYVVVKIPRW
     PFDKFGSADR TLGTQMKATG EVMAIDRTFE GALMKAVRSL EIGVDGLHLP GSAGWSEMEL
     EEKLSYPNDL RLFAIAEAFN RSWGMREVAQ LTTIDYFYLS KIRGIVELER ELQAAGPRPP
     RELLRRAKSC GLPDSLIGRL TGLPAREVHA LRKEYGILPA FKIVDTCAAE FEAVTPYYYS
     TYDDEDEVAV SGRPKVLVLG SGPIRIGQGI EFDYCSVHSV WGLQQEGIEA VIINNNPETV
     STDFDTADKL YFEPLTLEDV LNVIEKEKPL GVIVQFGGQT AINLTAGLAA LGVNILGTPV
     EGIDAAEDRD KFEKLLTGLG IPQSEGRSAV NVEEAQAVAE KLGYPVLVRP SYVLGGRAME
     IISSKTELVK YMTEAVQVSP RHPVLVDKYI RGKEVEVDAI GDGNDLFIPG IMEHIERAGV
     HSGDSIAVYP PQTLSREEID KIVEYTLKIG RALKINGLIN IQYVVDNGGV YVLEVNPRAS
     RTVPVLSKVT GVPMVQAATR AMLGRSLAEL GYRPGLGPVG GFIAVKAPVF SFEKLGLVEI
     SLGPEMKSTG EVMGIDRSFP GALYKAMRAA GLKVASGGRV VFSVADRDKA EAVSIAGEYA
     ALGYTLHATP GTARALEKAG LEVEVVEITD PVPLIRSGTV GLIINTPTRG KVPGRPGFLL
     RRTAAEYRVP CLTSLDTARA LAMVLRSVRW GGEPAPVSMA ELFEKEGTAN CCLRKKDSKA
     AIF
//
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