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 01-MAY-2013, entry version 60.
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=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 -!- 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; PMANLAT; -.
DR ProtClustDB; PRK05294; -.
DR BioCyc; MXAN246197:GIWU-3358-MONOMER; -.
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 1083 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_1000066373.
FT DOMAIN 133 328 ATP-grasp 1.
FT DOMAIN 679 871 ATP-grasp 2.
FT NP_BIND 159 216 ATP (By similarity).
FT NP_BIND 705 762 ATP (By similarity).
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 (By similarity).
FT METAL 299 299 Magnesium or manganese 1 (By similarity).
FT METAL 299 299 Magnesium or manganese 2 (By similarity).
FT METAL 301 301 Magnesium or manganese 2 (By similarity).
FT METAL 830 830 Magnesium or manganese 3 (By similarity).
FT METAL 842 842 Magnesium or manganese 3 (By similarity).
FT METAL 842 842 Magnesium or manganese 4 (By similarity).
FT METAL 844 844 Magnesium or manganese 4 (By similarity).
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
//
