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CARB_SULAC
ID   CARB_SULAC              Reviewed;        1052 AA.
AC   Q4J8E8;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=Saci_1620;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80932.1; -; Genomic_DNA.
DR   RefSeq; WP_011278434.1; NC_007181.1.
DR   AlphaFoldDB; Q4J8E8; -.
DR   SMR; Q4J8E8; -.
DR   STRING; 330779.Saci_1620; -.
DR   EnsemblBacteria; AAY80932; AAY80932; Saci_1620.
DR   GeneID; 3474176; -.
DR   KEGG; sai:Saci_1620; -.
DR   PATRIC; fig|330779.12.peg.1559; -.
DR   eggNOG; arCOG01594; Archaea.
DR   HOGENOM; CLU_000513_1_3_2; -.
DR   OMA; IEPAGIH; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001018; 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   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; PS00866; CPSASE_1; 1.
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..1052
FT                   /note="Carbamoyl-phosphate synthase large chain"
FT                   /id="PRO_0000145083"
FT   DOMAIN          131..325
FT                   /note="ATP-grasp 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          674..864
FT                   /note="ATP-grasp 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          930..1052
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   REGION          1..399
FT                   /note="Carboxyphosphate synthetic domain"
FT   REGION          400..548
FT                   /note="Oligomerization domain"
FT   REGION          549..930
FT                   /note="Carbamoyl phosphate synthetic domain"
FT   REGION          931..1052
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         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
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         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         700..757
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         823
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         835
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         835
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         837
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1052 AA;  117680 MW;  951DFCA441483727 CRC64;
     MRENVKRVLV IGSGPIKIAE AAEFDYSGSQ ALKALKEEGI ETILVNSNVA TVQTSRKFAD
     KLYMIPVTWW TVERVIEKER PDAIMIGFGG QTALNVGVDL YKKEILKKYG VKVLGTPIEG
     IERALSREKF RETMINVNLP VPPSLSARSE EEALEKARQI GYPVMVRVSF NLGGRGSTVA
     WSEEDLKRDI GRALSQSYIH EVLIEKYLHH WIELEYEVMR DKHGNSAVIA CIENLDPMGV
     HTGESTVIAP CQTLDNKEFQ DMRSMSIDVA KSIDLVGECN VQFALNPLAY EYYIIETNPR
     MSRSSALASK ATGYPLAYVS AKLALGYELY EVLNKVSGST CACFEPSLDY VVIKIPRWDL
     DKFENVEHSL ATEMKSVGEV MSIGRSFEEA LQKAVRMLDL GEPGIIGGKV YNSKMTKIDS
     LRMLKERRPY WFLYASKAFK EGATIDEVYE VTGINKFFLN KIKNLVDFYE SIKNNKGLDQ
     KTLSIAKRLG FSDYQIASAV GLSEKDIREL RQKYGIEPKV KQIDTLAGEW PAVTNYLYVT
     YNGTEDDIEF SNGIRKLLIV GAGGFRIGVS VEFDWGVVSL LDSASKYFDE VTIINYNPET
     VSTDWDIARK LYFDEISVER ILDLVRKEKF NYVATFAGGQ IGNTISKKLE ENGVKLLGTS
     GHSVDIAEDR EKFSRLLDKL GIKQPDWISA RSIEEVRKFV EMVGYPVLVR PSYVLSGSAM
     RIVYNDTELV SYIKKATEIS SEHPVVVSKY IDNAIEAEID GASDGRGVYG VVLEHVEEAG
     VHSGDATISI PFKKLSPETV HKMKESIHSI SRELNIKGPF NVQFVVKNGT PYIIEMNLRA
     SRSMPFSSKV VGKNIIDLAL TGVIKGFDFD EFVELKAKSW GVKSAQFSWA QLKGAYPFLG
     PEMRSTGEAA SLGVDFYDAL LKSWLSSSPN RLPDQKGIAL VYGRSNVEYL QASARNLSEY
     GMTVYTLSDA PIYGYEVTSS GKSVELIKDR KVEIVVTDGY LKSLDYEVRR IAVDYNVPII
     LNGRLGEELT KAFLLRKSNM TFYEIGEYGA GI
 
 
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