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 01-MAY-2013, entry version 37.
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; CITICNI; -.
DR ProtClustDB; CLSK2807444; -.
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 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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