GenomeNet

Database: UniProt
Entry: A1T8H1
LinkDB: A1T8H1
Original site: A1T8H1 
ID   CARB_MYCVP              Reviewed;        1112 AA.
AC   A1T8H1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   01-OCT-2014, entry version 61.
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=Mvan_2664;
OS   Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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: Binds 4 magnesium or manganese ions per subunit.
CC       {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}.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
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; CP000511; ABM13471.1; -; Genomic_DNA.
DR   RefSeq; WP_011779880.1; NC_008726.1.
DR   RefSeq; YP_953477.1; NC_008726.1.
DR   ProteinModelPortal; A1T8H1; -.
DR   STRING; 350058.Mvan_2664; -.
DR   PRIDE; A1T8H1; -.
DR   EnsemblBacteria; ABM13471; ABM13471; Mvan_2664.
DR   GeneID; 4644007; -.
DR   KEGG; mva:Mvan_2664; -.
DR   PATRIC; 18183593; VBIMycVan31953_2719.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; ARSAICH; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   BioCyc; MVAN350058:GIWR-2682-MONOMER; -.
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;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1112       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000066372.
FT   DOMAIN      138    333       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      693    884       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   NP_BIND     164    221       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     719    776       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    407       Carboxyphosphate synthetic domain.
FT   REGION      408    559       Oligomerization domain.
FT   REGION      560    965       Carbamoyl phosphate synthetic domain.
FT   REGION      966   1112       Allosteric domain.
FT   METAL       290    290       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       304    304       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       304    304       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       306    306       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       843    843       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       855    855       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       855    855       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       857    857       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1112 AA;  119326 MW;  92DD306569C57AEC CRC64;
     MPRRPDLNHV LVIGSGPILI GQAAEFDYSG TQACRVLRAE GLQVTLINSN PATIMTDPEY
     ADHTYVEPIT AEFVEKVIAQ QAERGNKIDA LLATLGGQTA LNTAVKLSEN GALERYGVEL
     IGADFEAIQR GEDRQKFKDI VTKVGGESAR SRVCFTMDEV RDTVADLGLP VVVRPSFTMG
     GLGSGMAYSA EDVERMAGDG LAASPSANVL IEESIYGWKE YELELMRDGH DNVVVVCSIE
     NFDPMGVHTG DSVTVAPAMT LTDREYQTMR TLGIEILREV GVDTGGCNIQ FAVNPKDGRL
     IVIEMNPRVS RSSALASKAT GFPIAKIAAK LAIGYTLDEI VNDITKETPA CFEPTLDYVV
     VKAPRFAFEK FPGADGTLTT TMKSVGEAMS LGRNFIEALG KVMRSLETGR AGFWTGPDPE
     GSVDEVLTRL HTATDGRLYD IEYALRLGAT VEQVAVASGV DPWFVEQIGR LVALRAELID
     APVLGEELLR RSKHNGLSDR QIAALRPELA GEMGVRVLRQ RLGIHPVFKT VDTCAAEFEA
     RTPYHYSSYE LDPSAETEVA PQAERPKVLI LGSGPNRIGQ GIEFDYSCVH AATTLTEAGF
     ETVMINCNPE TVSTDYDTAD RLYFEPLTFE DVLEIYYAEQ ASGEGGPGVV GVIVQLGGQT
     PLGLAERLEK AGVPIVGTLP EAIDLAEDRG EFGEVLRRAG LPAPRFGMAT SFDQARRIAA
     EIGYPVLVRP SYVLGGRGME IVYDEETLEG YITRATELSP EHPVLVDRFL EDAIEIDVDA
     LCDGTEVYIG GVMEHIEEAG IHSGDSACAL PPVTLGRSDI EAVRRATEAI AFGIGVVGLL
     NVQYALKDDV LYVLEANPRA SRTVPFVSKA TAVPLAKACA RIMLGATIAQ LREEGVLAST
     GDGAVTARNA PVAVKEAVLP FHRFRKADGS QIDSLLGPEM KSTGEVMGIA ADFGSAFAKS
     QTAAYGSLPA QGTVFVSVAN RDKRSLVFPV KRLADLGFRV LATEGTAEML RRNGIPCEEV
     RKHFQEFSEG LPQMSAVDAI KAGHVDMVIN TPYGNSGPRI DGYEIRSAAV SMNIPCVTTV
     QGASAAVQGI EAGIRGDIGV RSLQELHSAL GS
//
DBGET integrated database retrieval system