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Database: UniProt
Entry: B9KXM5
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Original site: B9KXM5 
ID   CARB_THERP              Reviewed;        1078 AA.
AC   B9KXM5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   14-MAY-2014, entry version 42.
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=trd_0212;
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E.,
RA   Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R.,
RA   Ward N.L., Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
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.
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DR   EMBL; CP001275; ACM05903.1; -; Genomic_DNA.
DR   RefSeq; YP_002521467.1; NC_011959.1.
DR   ProteinModelPortal; B9KXM5; -.
DR   STRING; 309801.trd_0212; -.
DR   EnsemblBacteria; ACM05903; ACM05903; trd_0212.
DR   GeneID; 7356430; -.
DR   KEGG; tro:trd_0212; -.
DR   PATRIC; 23911646; VBITheRos91376_0211.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; TFIDKWF; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   BioCyc; TROS309801:GI0S-210-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_A; CPSase_L_chain_A; 1.
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; Repeat.
FT   CHAIN         1   1078       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000164723.
FT   DOMAIN      133    327       ATP-grasp 1.
FT   DOMAIN      677    867       ATP-grasp 2.
FT   NP_BIND     159    216       ATP (By similarity).
FT   NP_BIND     703    760       ATP (By similarity).
FT   REGION        1    401       Carboxyphosphate synthetic domain.
FT   REGION      402    546       Oligomerization domain.
FT   REGION      547    935       Carbamoyl phosphate synthetic domain.
FT   REGION      936   1078       Allosteric domain.
FT   METAL       284    284       Magnesium or manganese 1 (By similarity).
FT   METAL       298    298       Magnesium or manganese 1 (By similarity).
FT   METAL       298    298       Magnesium or manganese 2 (By similarity).
FT   METAL       300    300       Magnesium or manganese 2 (By similarity).
FT   METAL       826    826       Magnesium or manganese 3 (By similarity).
FT   METAL       838    838       Magnesium or manganese 3 (By similarity).
FT   METAL       838    838       Magnesium or manganese 4 (By similarity).
FT   METAL       840    840       Magnesium or manganese 4 (By similarity).
SQ   SEQUENCE   1078 AA;  116728 MW;  54AB902F833C189D CRC64;
     MARQPLVSSV LVIGSGPIVI GQAAEFDYSG SQALRALREE GIRTIIVNSN PATIMTDEDM
     ADAVYIEPLT VEVLERIIAR ERPEGLLATL GGQTGLNLAV ALAEAGVLDR YGVRLLGTPL
     EAIRRAEDRQ LFKELLLEIG EPVLESLTAY SVEDALRFAE EVPPPLIVRP AFTLGGTGGG
     IAFSEDELVT LVQRGIAASP IGQVLVERSL LGWKEIEYEV MRDANDTCIT ICNIENLDPM
     GVHTGDSIVV APSQTLSDRD YQMLRSAALK IIRALGIVGG CNIQFALDPR SDQYYVIEVN
     PRVSRSSALA SKATGYPIAR IAAKLAIGRT LDEIPNPVTG KTMASFEPAL DYCVVKIPRW
     PFDKFRHGDR RLGSQMKATG EVMAIDRCFE AALQKAVRGL ETDQTDLTWE DSRWQDPSAL
     EQALRIPTDQ RLWAVAAALR RGWTPEHVSA LSGIDTWFVR AIQRLVEMEQ RLASEPLTAE
     LLWEAKRLGF ADRTIAALRT TTEQEIRAQR LALGLAPVYK LVDTCAAEFA AETPYFYATY
     EDENEAPPLD SPKAVVIGAG PIRIGQGIEF DYCSVKAAQA LHRAGVAAIM LNNNPETVST
     DFDASDRLYV TPLDAESVLD VLRHEASSQY DQLPPVIVQF GGQTAINLAA DLAAAGVPIL
     GTDQDAIDLA EDRRRFERFL HELGIPQPPG AGVTTLEEAL ETAERIGYPV LVRPSYVLGG
     RAMEVVYRRE HLEQYLATSG AFASGRPVLI DKYLDGIELE VDALCDGHEV LVPGIMQHIE
     RAGVHSGDSF AVYPAVELPS VHVDTLVRYT TEIALALAAR GLINIQFVLH QGVVYVLEVN
     PRASRTVPFL SKVTGVPMVD VATQILLGRS LGDQGYRGGL WPRQPLVAVK APVFSMAKLQ
     GVDVQLGPEM KSTGEAMGID RTFEAALAKA FLAAGLAIER GAPVLLSLAD NDKSAGVELA
     RGLLALGHPL VATEGTARYL RAHGVPVELT VAHIGHGHPD VLEVILERKV RGVINTPGRD
     EGTIQDGFLI RRAAVERGIP CLTSLDTARA LVRALLGGGT SFSVQPLPAY RTREAVLA
//
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