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-MAY-2013, entry version 55.
DE RecName: Full=Carbamoyl-phosphate synthase large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=carB; 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 -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC carbamoyl phosphate from bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
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 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the CarB family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
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; 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; SEFFEIV; -.
DR ProtClustDB; PRK05294; -.
DR BioCyc; MVAN350058:GIWR-2682-MONOMER; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA: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; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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; Repeat.
FT CHAIN 1 1112 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_1000066372.
FT DOMAIN 138 333 ATP-grasp 1.
FT DOMAIN 693 884 ATP-grasp 2.
FT NP_BIND 164 221 ATP (By similarity).
FT NP_BIND 719 776 ATP (By similarity).
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 (By similarity).
FT METAL 304 304 Magnesium or manganese 1 (By similarity).
FT METAL 304 304 Magnesium or manganese 2 (By similarity).
FT METAL 306 306 Magnesium or manganese 2 (By similarity).
FT METAL 843 843 Magnesium or manganese 3 (By similarity).
FT METAL 855 855 Magnesium or manganese 3 (By similarity).
FT METAL 855 855 Magnesium or manganese 4 (By similarity).
FT METAL 857 857 Magnesium or manganese 4 (By similarity).
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
//
