GenomeNet

Database: UniProt
Entry: B7GPW2
LinkDB: B7GPW2
Original site: B7GPW2 
ID   CARB_BIFLS              Reviewed;        1127 AA.
AC   B7GPW2; E8MQR7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 67.
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=Blon_0738, BLIJ_0750;
OS   Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088
OS   / JCM 1222 / NCTC 11817 / S12).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=391904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA   Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA   Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA   Richardson P.M., Mills D.A.;
RT   "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT   adaptations for milk utilization within the infant microbiome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K.,
RA   Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K.,
RA   Kikuchi J., Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
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; CP001095; ACJ51842.1; -; Genomic_DNA.
DR   EMBL; AP010889; BAJ68342.1; -; Genomic_DNA.
DR   RefSeq; WP_012577127.1; NZ_JDTT01000007.1.
DR   ProteinModelPortal; B7GPW2; -.
DR   SMR; B7GPW2; -.
DR   PRIDE; B7GPW2; -.
DR   EnsemblBacteria; ACJ51842; ACJ51842; Blon_0738.
DR   EnsemblBacteria; BAJ68342; BAJ68342; BLIJ_0750.
DR   KEGG; bln:Blon_0738; -.
DR   KEGG; blon:BLIJ_0750; -.
DR   PATRIC; fig|391904.8.peg.754; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   BioCyc; BLON391904:G1H61-749-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001360; 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   CDD; cd01424; MGS_CPS_II; 1.
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; 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   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT   CHAIN         1   1127       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000164708.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      681    881       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      964   1127       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     707    773       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    553       Oligomerization domain.
FT   REGION      554    962       Carbamoyl phosphate synthetic domain.
FT   REGION      963   1127       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       840    840       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       852    852       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       852    852       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       854    854       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1127 AA;  123087 MW;  B19EA0289F83D6D2 CRC64;
     MPKRTDIKSV MVIGSGPIVI GQAAEFDYSG TQACRVLREE GIRVILVNSN PATIMTDPEM
     ADATYIEPIA TPILEQIIAK ERPDALLPTL GGQTALNAAM ALGEAGVLKK YNVELIGASL
     EAIDRGEDRE LFKKVVDEAG AESARSDIAH SIEEVDKIAE KFGYPLVVRP SFTMGGLGSG
     IAHNEEELHR IAGAGIHYSP TDEVLIEEGI EGWKEFELEL MRDRNDNVVV VCPIENVDPV
     GVHTGDSITV APCFTLTDRE YQKLRDIGIA IIRGVGVDTG GCNIQFAVHP KTGRIIVIEM
     NPRVSRSSAL ASKATGFPIA KIATKLALGY TLDEIRNDIT QSTPASFEPT IDYVVTKVPR
     FAFEKFPGAD PTLTTSMKSV GEAMALAGNF QESLGKAMRS IDKRHMGFNW DGEKPSAEEV
     AELLEAIHTP TEHRYLQLMR AIWGGATLEQ VFAATKIDPW FLKQIFLINE TAMTVREAET
     LTPKLLKKAK LAGLSDVQVA HLRGLGDEGE NTIRELRWTY GLRPVYKTVD TCAAEFDAAT
     PYYYSCYADE TELRPREREA VIILGSGPNR IGQGIEFDYT CVHAVQELGK DYDTIMVNCN
     PETVSTDYDM SDRLYFEPLT FEDVLEIYEA EKKMGPVKGI IVQLGGQTPL SLAARLKAAG
     VPILGTTPES IDLAENRELF GEVLKKAEMN APRYGTALSL EEAMDAAHRI GYPVLVRPSY
     VLGGRGMEIV YDDKQLTKYV DRALAEAKAD TVVSGRLPSP LLIDKFLQDA IEIDVDALFD
     GEELYIGGIM EHVEEAGVHS GDAACTLPPS TLSDDQIRRL REGTYAIAKG CHVQGLINVQ
     YAFMANTLYV IEANPRASRT VPFASKATGV ALAKAAARIM AGETIADQRA NGLLLPKGDG
     GDIHPGQQVA VKESVLPFKR FRTPVGKTVD ILLGPEMRST GEVMGFDRDF PHAFAKSQLA
     AYDGGLPTHG NVFISVNDTD KRQLPLIAVR LEELGFKIWA TEGTASVLSR YGIESNIVDK
     ISTRVDTDPE APVEVHHAAG SVGKNVVDLI EEGKIDMILN TPNSRGSRSD GYSIRAAAIA
     ADLPQFTTIT EFQAALLAIE AVKHNDYQIM SIQEHSKQLF ELERREF
//
DBGET integrated database retrieval system