GenomeNet

Database: UniProt
Entry: B2G564
LinkDB: B2G564
Original site: B2G564 
ID   CARB_LACRJ              Reviewed;        1056 AA.
AC   B2G564;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   05-DEC-2018, entry version 71.
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=LAR_0080;
OS   Lactobacillus reuteri (strain JCM 1112).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H.,
RA   Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H.,
RA   Kikuchi J., Masaoka T., Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and
RT   Lactobacillus fermentum reveal a genomic island for reuterin and
RT   cobalamin production.";
RL   DNA Res. 15:151-161(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; AP007281; BAG24596.1; -; Genomic_DNA.
DR   RefSeq; WP_003669623.1; NC_010609.1.
DR   ProteinModelPortal; B2G564; -.
DR   SMR; B2G564; -.
DR   EnsemblBacteria; BAG24596; BAG24596; LAR_0080.
DR   GeneID; 5189817; -.
DR   KEGG; lrf:LAR_0080; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   BioCyc; LREU557433:G1G2C-87-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
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   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.40.50.1380; -; 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; 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; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Repeat.
FT   CHAIN         1   1056       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000138894.
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   1056       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   1056       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   1056 AA;  116836 MW;  1506026959D96636 CRC64;
     MPKRTDIHKI LVIGSGPIII GQAAEFDYSG TQACLALREE GYETILVNSN PATIMTDKEI
     ADHVYIEPLT VESLSRIIRQ EYPDAILPTL GGQIGLNLAV SLSETGLLDE LGIELLGTKL
     DSIDEAEDRE KFKELMNELG EPVPASQTVN TVDEAVEFAH QCGYPVIVRP AFTMGGTGGG
     ICHNDAEMRT VAKNGLELSP VTQCLIEKSI AGYKEIEFEV MRDAADNVMV VCCMENFDPV
     GIHTGDSIVF APNQTLSDRE YQMLRDCALK LIRALKIEGG CNVQLALDPQ SFQYNVIEVN
     PRVSRSSALA SKATGYPIAK MAAKIAVGLT LDEIKNPVTK TTFAEFEPAL DYVVCKIPRW
     PFDKFTQADR HLGSQMKATG EVMAIGRTAE EALHKAVRSL EIDEKDLFSA EAHHAPTDML
     EKKLRYPQDD RLFYLAETFR RGYSLQQTHD LTKISPYFLD IVKHLVELED DLSTKPFDVE
     TLITSKKYGF SDATIARLWH TSSQEVRKFR KQNEVLPVYK MIDTCAAEFA SSTPYFYSAY
     DHENESQRTK KPSILVLGSG PIRIGQGVEF DYATVHSVKA IQRAGYEAIV INSNPETVST
     DFSVSDKLYF EPLTLEDVLN VIDLEQPVGV IVQFGGQTAI NLAEGLAKNG VNILGTTVDD
     LDAAEDREVF DQVITDLNLK QPIGLTATTH SAVIKAAEKI GYPVLVRPSY VLGGKAMETV
     YNQEELQQYL QQNASITADH PILIDAYLEG RECEVDAICD GKDVLIPGIM EHIEHAGVHS
     GDSMAVYPPQ HFNDDIKRQI VTATEKLAVA LKCIGIMNIQ FIVHNHEVYI LEVNPRASRT
     VPFLSKITGI EMAQVATRVI LGQSLADQGF TNGLYPEPQT IHVKAPVFSF NKLANVDSYL
     SPEMKSTGEV MGTDTTYEKA LHKAFSGAHI QVPNDGKILF TIENGDEKEV LPLAKRFAQI
     GYQVFTTPQT ASHFKDNGIH IHQEISNIDE LNCLLKAGQI DLVINTMRHD YEQDSLGFQI
     RQSTIAQNVP LMTSLDTVNA LLRVKEDQSL EAITIK
//
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