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Database: UniProt
Entry: O50302
LinkDB: O50302
Original site: O50302 
ID   CARB_GEOSE              Reviewed;        1064 AA.
AC   O50302;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   05-DEC-2018, entry version 99.
DE   RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific large chain;
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=pyrAB;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCM 2184;
RX   PubMed=10732707;
RA   Vlaskova H., Krasny L., Fucik V., Jonak J.;
RT   "The pyrAb gene coding for the large subunit of carbamoylphosphate
RT   synthetase from Bacillus stearothermophilus: molecular cloning and
RT   functional characterization.";
RL   Folia Biol. (Praha) 44:163-172(1998).
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: 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   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
DR   EMBL; AJ001805; CAA05020.1; -; Genomic_DNA.
DR   PIR; T44419; T44419.
DR   ProteinModelPortal; O50302; -.
DR   SMR; O50302; -.
DR   PRIDE; O50302; -.
DR   BRENDA; 6.3.5.5; 623.
DR   UniPathway; UPA00070; UER00115.
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   ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT   CHAIN         1   1064       Carbamoyl-phosphate synthase pyrimidine-
FT                                specific large chain.
FT                                /FTId=PRO_0000144989.
FT   DOMAIN      133    327       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      671    861       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      930   1064       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     697    754       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    401       Carboxyphosphate synthetic domain.
FT   REGION      402    546       Oligomerization domain.
FT   REGION      547    929       Carbamoyl phosphate synthetic domain.
FT   REGION      930   1064       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       820    820       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       832    832       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       832    832       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       834    834       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1064 AA;  116243 MW;  F5AD61003AA3FC4B CRC64;
     MPKRRDIETI LVIGSGPIVI GQAAEFDYAG TQACLALKEE GYKVILVNSN PATIMTDTEI
     ADKVYMEPLT LDFVARIIRK ERPDAILPTL GGQTGLNLAV ELAKAGVLEE CGVEILGTKL
     EAIEKAEDRE QFRALMNELG EPVPESAIIH SLEEAYAFVE QIGYPVIVRP AFTLGGTGGG
     ICTNEEELVE IVSTGLKLSP VHQCLLERSI AGYNQIEYEV MRDANDNAIV VCNMENIDPV
     GIHTGDSIVV APSQTLSDRE YQLLRNASLK IIRALGIEGG CNVQLALDPD SFRYYVIEVN
     PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMINPVTG KTYACFEPAL DYVVTKIPRF
     PFDKFESANR RLGTQMKATG EVMSIGRTFE ESLLKAVRSL EIGVHHLELN EAKTAADDVM
     EKRIRKAGDE RLFYIAEALR RGVTVETLHE WSQIDRFFLH KIQNIIEMET VLKNHPGDLD
     VLKKAKGLGF SDAAIAALWN KTERDVYALR RQEGIVPVYK MVDTCAAEFT SETPYYYSTY
     EEENESIVTE KPSVIVLGSG PIRIGQGIEF DYATVHCVLA IKQAGYEAII INNNPETVST
     DFSTSDKLYF EPLTAEDVMH VIDLEQPVGV IVQFGGQTAI NLAAELEARG VRLLGTTLED
     LDRAEDRDKF EQALSELGIP KPAGKTAVSV EEAVAIAEEI GYPVLVRPSY VLGGRAMEIV
     YNREELLHYM EHAVRVNPQH PVLVDRYITG KEVEVDAIAD GETVVIPGIM EHIERAGVHS
     GDSIAVYPPQ TLSDDVIAKI TDYTVKLARG LHIVGLLNIQ FVVAGSDVYV LEVNPRSSRT
     VPFLSKITGV PMANLATKAI LGAKLADMGY ETGVCPVRPG VYVKVPVFSF AKLRNVDISL
     GPEMKSTGEV IGKDVTFEKA LYKGLVASGI QIQPHGAVLL TVADKDKEEA VELARRFADI
     GYQLLATNGT AETLKAAGIP VTVVNKIHSA SPNILDVIRQ GKAQVVINTL TKGKQPESDG
     FRIRREVENG IPCLTSLDTA RAMLQVLESM TFSTTAMTEG LVRS
//
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