GenomeNet

Database: UniProt
Entry: A6WCC6
LinkDB: A6WCC6
Original site: A6WCC6 
ID   CARB_KINRD              Reviewed;        1104 AA.
AC   A6WCC6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   16-JAN-2019, entry version 81.
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=Krad_3001;
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 /
OS   SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=266940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E.,
RA   Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Lykidis A., Bagwell C.E.,
RA   Shimkets L., Berry C.J., Fliermans C., Richardson P.;
RT   "Complete sequence of chromosome of Kineococcus radiotolerans
RT   SRS30216.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000750; ABS04465.1; -; Genomic_DNA.
DR   RefSeq; WP_012087288.1; NC_009664.2.
DR   ProteinModelPortal; A6WCC6; -.
DR   SMR; A6WCC6; -.
DR   STRING; 266940.Krad_3001; -.
DR   PRIDE; A6WCC6; -.
DR   EnsemblBacteria; ABS04465; ABS04465; Krad_3001.
DR   KEGG; kra:Krad_3001; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   OrthoDB; 48855at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001116; Chromosome.
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   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.40.50.1380; -; 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   1104       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000085558.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      676    867       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      949   1099       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     702    759       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    547       Oligomerization domain.
FT   REGION      548    948       Carbamoyl phosphate synthetic domain.
FT   REGION      949   1104       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       826    826       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       838    838       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       838    838       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       840    840       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1104 AA;  117821 MW;  DA1F2C985C4A959B CRC64;
     MPRRTDLKSV LVIGSGPIVI GQAAEFDYSG TQACRVLRAE GLRVILVNSN PATIMTDPEM
     ADATYVEPIT PAVVEAIIAK ERPDAVLATL GGQTALNTAI ALYENGVLEK YGTELIGADV
     EAIKLGEDRQ LFKGVVERCG AESARSHLCH SMEEVLAGAA DLGYPVVVRP SFTMGGLGSG
     FAYDEADLRR IAGQGLHHSP VTEVLLEESI LGWKEYELEL MRDRADNVVV VCSIENFDPM
     GVHTGDSITV APAMTLTDRE YQRMRDIGIA VIREVGVDTG GCNIQFAVNP EDGRIIVIEM
     NPRVSRSSAL ASKATGFPIA KIAARLAVGY TLDEIPNDIT SSTPASFEPT LDYVVVKVPR
     FAFEKFPAAD PTLTTTMKSV GEAMALGRNF TEALQKALRS TEKRGATFSW AGEPGDRADL
     LRRAAQPTDE RIGLVMQAIR AGATPEELFE STRIDPWFLD QMFLLDEIAG EVRDSDELTP
     ELLRHAKRHG FSDAQIGELR HLPEDVVRGV RHALGIRPVY KTVDTCAAEF AASTPYHYSS
     YDEEDETRPR EKAAIVILGS GPNRIGQGVE FDYSCVHASF ALRDAGYETV MVNCNPETVS
     TDYDTSDRLY FEPLTLEDVL EVVHAEMRCG PVAGVIVQLG GQTPLGLAAK LEQAGVPIIG
     TSPQAIDLAE ERGAFGQVLE RAGLVAPKHG TASSFPGAKA IAAGIGYPVL VRPSYVLGGR
     GMQIVYDEAS LEEYMRTATE VSPERPVLVD RFLDDAIEID VDALFDGEEM YLGGIMEHIE
     EAGIHSGDSA CVIPPPTLGN AELARVRAAT EAIARGVGVR GLLNVQFALA ADVLYVLEAN
     PRASRTVPFV SKATGVALAK AAARLMAGTS IRDLRAEGLL PGRGDGGLLP ADSPVSVKEA
     VLPFARFRTA EGVVVDSLLG PEMRSTGEVM GIDVDFPTAF GKSQTAAYGG LPTAGTAFIS
     VADRDKRAMI FPIKRLADLG FTLVATEGTA QVLRRNGITS TVVRKHSEGT SEDGELTIVG
     RIGAGEIAMV VNTPSGNQAR ADGYEIRAAA TAVGSPIITT IQELSAAVQA IEAAIVQERN
     GGGVNVASLQ EHTARLNAAW EGRA
//
DBGET integrated database retrieval system