GenomeNet

Database: UniProt
Entry: Q59599
LinkDB: Q59599
Original site: Q59599 
ID   CARB_NEIGO              Reviewed;        1071 AA.
AC   Q59599;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   26-NOV-2014, entry version 89.
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};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CH811;
RX   PubMed=7773412;
RA   Lawson F.S., Billowes F.M., Dillon J.A.;
RT   "Organization of carbamoyl-phosphate synthase genes in Neisseria
RT   gonorrhoeae includes a large, variable intergenic sequence which is
RT   also present in other Neisseria species.";
RL   Microbiology 141:1183-1191(1995).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC       {ECO:0000255|HAMAP-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   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA74996.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U11295; AAA74996.1; ALT_FRAME; Genomic_DNA.
DR   ProteinModelPortal; Q59599; -.
DR   PRIDE; Q59599; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 2.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
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.
DR   Pfam; PF00289; CPSase_L_chain; 2.
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; 1.
DR   PROSITE; PS00867; CPSASE_2; 2.
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   1071       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145024.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      673    864       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     699    756       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    403       Carboxyphosphate synthetic domain.
FT   REGION      404    548       Oligomerization domain.
FT   REGION      549    930       Carbamoyl phosphate synthetic domain.
FT   REGION      931   1071       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       823    823       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       835    835       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       835    835       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       837    837       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1071 AA;  117584 MW;  04B99981D3EB8212 CRC64;
     MPKRTDLKSI LIIGAGPIVI GQACEFDYSG AQACKALREE GYKVILVNSN PATIMTDPEM
     ADVTYIEPIM WQTVEKIIAK ERPDAILPTM GGQTXLNCAL DLAGNGVLAK YDVELIGATE
     DAIDKAEDPG RFKEAMEKIG LSCPKSLFCH TMNEALAAQE QVGFPTLIRP SFTMGGSGGG
     IAYNKDEFLA ICERGFDASP THELLIEQSV LGWKEYEMEV VRDKADNCII ICSIENFDPM
     GVHTGDSITV APAETLTDKE YQIMRNASLA VLREIGVDTG GSNVQFAVNP EKGEMIVIEM
     NPRVSRSSAL ASKATGFPIA KVAANWAVGF TLDELRNDIT GRRTPASFEP SIDYVVTKMA
     RFAFEKFPAA DDRLTTQMKS VGEVMAMGRT IQESFQKALR GLETGLCGFN PARRRQTEIR
     RELANPGPER MLFVGKAFRA AFTPEEIHEI SAIDPWFLAQ IEDLMKEEKS VSDGQLQDLD
     YAALHRLKRK GFSDKRLAQL LNVSEKEVRE TRTPVKLDPV YKPVDTSAAE FATETAYLYS
     TYEEECESRP SDRKKVMILG AGPNPIGQGI EFDYCSVHAA LPLRESGFET IMVNCNPETV
     STDFDTSDRL YFEPLTLEDV LEIVRTENPW GVIVHYGGQT PLKLANALVE NGVNIIGTSA
     DSIDAAEDRE RFQKVLNDLG LRQPPNRIAH NEEEALVKAE EIGYPLVVRP SYVLGGPAMQ
     IVHSAEALQK YMREPVQVSE DSPVLLDFFL NNAIEVDVDC VSDGKDVVIG GIMQHVEQAG
     IHSGDSGCSL PPYSLSEEIQ DEIRRQTKAM AYALGLVGLM NVQFAVQDAV VFVLEVNPRA
     TRTVPFVSKA TGQRLAKVGA RCMAGISLKE QGVEKEVVPD FYAVKEAVFP FIKFPGVDTI
     LNPEMRSTGE VMGVGRSFGE AYYKAQLGAG ERLNPTGKIF LSVREEDKER VIKTAKNFQA
     LGYGICPTRG TAQYLTEHGL IVQAINKVPE GRPHIGDALK NGEIALVVNT VSSDPQSVSD
     SHIIRQSALQ QRVPQYTTTA GGEAMSEGAK SRDYLGVYSV QELHGRLKNR N
//
DBGET integrated database retrieval system