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Database: UniProt
Entry: Q1D6Y8
LinkDB: Q1D6Y8
Original site: Q1D6Y8 
ID   CARB_MYXXD              Reviewed;        1083 AA.
AC   Q1D6Y8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   26-NOV-2014, entry version 66.
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=MXAN_3388;
OS   Myxococcus xanthus (strain DK 1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK 1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC       {ECO:0000255|HAMAP-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}.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
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DR   EMBL; CP000113; ABF92803.1; -; Genomic_DNA.
DR   RefSeq; YP_631585.1; NC_008095.1.
DR   ProteinModelPortal; Q1D6Y8; -.
DR   STRING; 246197.MXAN_3388; -.
DR   PRIDE; Q1D6Y8; -.
DR   EnsemblBacteria; ABF92803; ABF92803; MXAN_3388.
DR   GeneID; 4107498; -.
DR   KEGG; mxa:MXAN_3388; -.
DR   PATRIC; 22649319; VBIMyxXan43560_3332.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; GSDRIWY; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   BioCyc; MXAN246197:GIWU-3358-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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-UniPathway.
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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1083       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000066373.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      679    871       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     705    762       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    554       Oligomerization domain.
FT   REGION      555    937       Carbamoyl phosphate synthetic domain.
FT   REGION      938   1083       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       830    830       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       842    842       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       842    842       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       844    844       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1083 AA;  118757 MW;  D392D0CBE6321903 CRC64;
     MPKRTDIRKV LVIGSGPIVI GQAVEFDYSG TQAIKALRDE GVEVVLLNSN PATVMTDPEF
     AHRTYIEPIT VEAAERILAS ERPDSLLPTM GGQTALNLAK ALAEQGILEK YGVRLIGASL
     DAINKAEDRQ LFKAAMQKIG VALPKSGYAT TLDQAMSLVE DIGFPAIIRP SFTLGGTGGG
     IAYNREEFET ICRSGLKASP TTTILVEESV LGWKEYELEV VRDTADNVII VCSIENLDPM
     GVHTGDSITV APAQTLTDRE YQRMRQASLA IIREIGVETG GSNIQFGINP KDGRMVVIEM
     NPRVSRSSAL ASKATGYPIA KIAAKLALGY TLDELRNDIT RDTPASFEPT LDYVVVKVPR
     FNFEKFPHAD RTLTTSMRSV GEVMAIGRTF PEAYMKALRS MELGRVGLES PELPAEKEER
     EKVLREALRI PRPERPWFVA QAFREGMTVE DVHALSAIDP WFLRYIQMLV NEAQSLQEYG
     RLDQLPDEVL RQAKAHGFSD KYLGRLLGYP AEEVRAHRHA RNIRPVYKRV DTCAAEFEAY
     TPYLYSTYEE EDEAPPTDRQ KVLILGSGPI RIGQGIEFDY ACVHAAFALR EAGYETVMVN
     CNPETVSTDY DTSDRLYFEP LTIEDVLEVS QREKPVGAIV QFGGQTPLRI SVPLEKAGLP
     ILGTSPDAID RAEDRERFAA LIEKLGLKQP ENGVARSHAE AFKVAERIGY PVMVRPSYVL
     GGRAMETVYD VASLERYMRE AVSASPEHPV LIDRFLKEAI EVDLDLVADR TGAVMIGGVL
     EHIQEAGVHS GDAAATLPPH SLSPDLVERM KDQAIALARE LGVVGLMNVQ FAIQGKTIYI
     LEVNPRASRT VPFISKATGV AMAKIAALCM VGKTLKELGV TQEPEFKHVA VKESVFPFAR
     FAGVDVILGP EMKSTGEVMG LANDYASAFA KSQLAAGVKL PKSGKVFISV KDDDKPAVVD
     LARRLRSMGF SLVVTSGTHT YLATKGIEAQ VVQKVTEGRP NIVDKIVDGE IVLVINTTFG
     KQEIADSFSI RRESLMHSVP YYTTVQAARM AVGALESLKC TELEVKPLQE YLGINAAPPG
     TRR
//
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