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Database: UniProt
Entry: Q9WZ27
LinkDB: Q9WZ27
Original site: Q9WZ27 
ID   CARB_THEMA              Reviewed;        1099 AA.
AC   Q9WZ27;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   13-FEB-2019, entry version 141.
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=TM_0557;
OS   Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
RA   Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
RA   McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
RA   Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
RA   Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
RA   Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000255|HAMAP-
CC         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       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
DR   EMBL; AE000512; AAD35642.1; -; Genomic_DNA.
DR   PIR; C72363; C72363.
DR   RefSeq; NP_228367.1; NC_000853.1.
DR   RefSeq; WP_004081324.1; NZ_CP011107.1.
DR   ProteinModelPortal; Q9WZ27; -.
DR   SMR; Q9WZ27; -.
DR   STRING; 243274.TM0557; -.
DR   PRIDE; Q9WZ27; -.
DR   EnsemblBacteria; AAD35642; AAD35642; TM_0557.
DR   GeneID; 897615; -.
DR   KEGG; tma:TM0557; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   InParanoid; Q9WZ27; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 48855at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
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; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
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; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR033937; MGS_CPS_CarB.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
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; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 1.
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   1099       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145058.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      666    857       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      945   1099       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     692    749       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    541       Oligomerization domain.
FT   REGION      542    944       Carbamoyl phosphate synthetic domain.
FT   REGION      945   1099       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       816    816       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       828    828       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       828    828       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       830    830       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1099 AA;  121317 MW;  C2D51E7F649BBAE5 CRC64;
     MPKREDIKRI LVIGSGPITI GQAAEFDYSG TQALKALKSA GYEVIIVNSN SATIMTDPEF
     SDAVYIEPLT VEFLEKIIEK ERPDALLPTL GGQTALNLAV ELAERGILDK YGVQLIGAKL
     ESIKKAEDRE LFKETMEKAG LEVLRSRLVN NLADALETAR EFGYPVIIRP SFTLGGTGGG
     IAFNEEELRD IVTKGLIESP VHTVLIEESV LGWKEYELEV VRDGAGNFIV VCSIENLDPM
     GIHTGDSITV APAQTLTDVE YQRMRDAAYK VIDAIGIETG GSNIQFALDP ETGRMVVIEM
     NPRVSRSSAL ASKATGYPIA KVAALLAVGF TLDEIPNYIT GKTMAAFEPS IDYVVVKIPR
     FQLEKFPGAD PRLNTQMKSV GEVMAIGRTF KEALGKALRS LELDAAPKLD LEHIREHLAN
     PTPERISYVF AAFRNGMDVE EVHELTKIDR WFLREMKACI ELEEELKLKK FDVEILKKAK
     QWGYSDREIA EIWGVSEKEI RKMREDNRIF PVYKMVDTCA AEFEAQTPYY YSTYNGVENE
     AVPSDREKIM ILGSGPNRIG QGIEFDYTNV HGVWSFQEEG YETIMVNSNP ETVSTDYDTS
     DRLYFEPLTV EDVLEIVRNE KPKGVVVAFG GQTPLKIAKY LVEERVNIIG TSFESIEIAE
     DREKFAKLLK QIGLKCPPFG TASSVEEALR VAENLGYPVL VRPSYVLGGR AMAIVDTPQE
     LEMYVKEAAV VSPGYPVLID KFLEDAIELD VDVVSDGKYV WIAGLMEQIE EAGVHSGDSA
     CVLPPVSLSE KLVEEIEETV YKLVKALKVV GVANIQLAVK DEEIYIIEAN PRASRTVPFV
     SKAIGIPVAR IAAKIMVGRN LPELLSEYFP YPTRPGVKVD KLGESEILPT PWPKMFSVKE
     VVIPFHKFPG TDVLLGPEMR STGEVMGIGE DFAEAFAKAQ IAAGNPLPTT GAILATVADK
     DKREAVPLLA HLADMGFEIY ATRGTAKALQ SHGVEVKVVP KVGEGRPDVI DLLEQGKISL
     VVITQSSDEP ALVAVSHGKE PFKVEGRRTV GYMIRTTALK RKIPYLTTVE SLRAAVAAIR
     KMKKGSIVKV RRLTDTWKM
//
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