CARB_PYRAE
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 03-AUG-2022, entry version 135.
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=PAE0947;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
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; 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; AE009441; AAL63148.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZY48; -.
DR SMR; Q8ZY48; -.
DR STRING; 178306.PAE0947; -.
DR EnsemblBacteria; AAL63148; AAL63148; PAE0947.
DR KEGG; pai:PAE0947; -.
DR PATRIC; fig|178306.9.peg.701; -.
DR eggNOG; arCOG01594; Archaea.
DR HOGENOM; CLU_000513_1_3_2; -.
DR InParanoid; Q8ZY48; -.
DR OMA; IEPAGIH; -.
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; IPR011607; MGS-like_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; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..1024
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145081"
FT DOMAIN 129..323
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 660..849
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 917..1024
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..396
FT /note="Carboxyphosphate synthetic domain"
FT REGION 397..536
FT /note="Oligomerization domain"
FT REGION 536..917
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 918..1024
FT /note="Allosteric domain"
FT BINDING 155..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 686..743
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 809
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="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
