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Database: UniProt
Entry: Q8ZY48
LinkDB: Q8ZY48
Original site: Q8ZY48 
ID   CARB_PYRAE              Reviewed;        1024 AA.
AC   Q8ZY48;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   13-FEB-2019, entry version 124.
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=PAE0947;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630
OS   / NBRC 100827).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL63148.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8ZY48; -.
DR   SMR; Q8ZY48; -.
DR   STRING; 178306.PAE0947; -.
DR   PRIDE; Q8ZY48; -.
DR   EnsemblBacteria; AAL63148; AAL63148; PAE0947.
DR   KEGG; pai:PAE0947; -.
DR   PATRIC; fig|178306.9.peg.701; -.
DR   eggNOG; arCOG01594; Archaea.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234583; -.
DR   InParanoid; Q8ZY48; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002439; 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   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00867; CPSASE_2; 1.
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   1024       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145081.
FT   DOMAIN      129    323       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      660    849       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      917   1024       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     155    212       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     686    743       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    396       Carboxyphosphate synthetic domain.
FT   REGION      397    536       Oligomerization domain.
FT   REGION      536    917       Carbamoyl phosphate synthetic domain.
FT   REGION      918   1024       Allosteric domain.
FT   METAL       280    280       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       294    294       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       294    294       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       296    296       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       809    809       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       820    820       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       820    820       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       822    822       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1024 AA;  113140 MW;  ED2317D63BD64E03 CRC64;
     MDIKKILVIG SGAIKVAEAA EFDYSGSQAL KAFREEGIKT VLVNPNIATI QTSKFLADRV
     YFIPIQRQFL AEVIEQERPD AIACGFGGQT ALSACVDLDE AGVLEKYGVR VVGTPVRGIK
     RALSRDLFQK AMREAGIPVP PSSPAKSPEE AIEIARYLGY PVVVRVSFNL GGAGAFVARS
     EEALKARIYK AFAQSAIGEV LVEKYLEGWK EIEFEVVRDA YDNVAAVVCM ENIDPMGVHT
     GDSIVVAPCL TLTDEEYQTA RNISIGVVRT IELIGEGNVQ VAINYAGPEQ YAIETNPRMS
     RSSALASKAS GYPLAYIAAK LALGYRLDEV LNQVTRRTVA SFEPALDYIV VKHPRWESDR
     FGVTEGLGPE MMSIGEAMGI GRTLEEAWQK AVRMIDIGEP GLVGGPMFQS LTLEEALKCI
     KDYVPYWPIC AAKAIYLGVS VEEIYKINKV DKFFLNAIKR IVDVYKRLEA GEVDLDEAKV
     LGFSDWQIAK ALGKSVDEIR AMRRRPVVKK IDTLAGEWPA DTNYLYLTYG GQYDDKTPGV
     DYLVVGAGVF RIGVSVEFDW STVTLATELK NRGYRVAILN YNPETVSTDW DIVDKLYFDE
     ISVERVLDIV EKEGNGVTVV LYAGGQIGQR LYVPLEKVGV KIGGTRAKSI DMAEDRGKFS
     KLLDRLGIKQ PPWLYAASVE EAVKLAEGLG FPVLLRPSYV LGGTYMAVAY NKEELINFLS
     KAAKVSGEYP VVISKFMPRG IEAEVDAVSD GVKIVATPIE HIEPPGVHSG DSTMVLPPRR
     LEEWAVKKMI DIAHTLAVEL EVKGPLNVQF IVQDDVYVIE ANLRVSRSMP LVSKATGVNY
     MSLVADVLTH GRLAVDEERI TLKPSKWWVK SPQFSWARLR GAYPRLGPVM YSTGEVASNG
     SVFEEALLKS WLSATPNKIP SKTALIYTYD PHHEELLRQA AGLLSWRLEI YTPEQLGGKI
     AEMLKWRKID IVMTAGITPE KDFHVRRTAA DTNTPLVLDS TLAVELAKAF NWYYKNGKLE
     VAPW
//
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