(data stored in ACNUC7421 zone)

HOGENOM: POLSQ_1_PE1012

ID   POLSQ_1_PE1012                       STANDARD;      PRT;   1087 AA.
AC   POLSQ_1_PE1012; A4SXM0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Carbamoyl-phosphate synthase large chain; EC=6.3.5
DE   5;AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
DE   (POLSQ_1.PE1012).
GN   Name=carB; OrderedLocusNames=Pnuc_1018;
OS   POLYNUCLEOBACTER NECESSARIUS SUBSP. ASYMBIOTICUS QLW-P1DMWA-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS POLSQ_1.PE1012.
CC       Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1, complete
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:A4SXM0_POLSQ
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   -!- GENE_FAMILY: HOG000234582 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A4SXM0; -.
DR   EMBL; CP000655; ABP34234.1; -; Genomic_DNA.
DR   RefSeq; YP_001155798.1; NC_009379.1.
DR   ProteinModelPortal; A4SXM0; -.
DR   STRING; A4SXM0; -.
DR   GeneID; 5052878; -.
DR   GenomeReviews; CP000655_GR; Pnuc_1018.
DR   KEGG; pnu:Pnuc_1018; -.
DR   eggNOG; COG0458; -.
DR   OMA; QGVTKEI; -.
DR   PhylomeDB; A4SXM0; -.
DR   ProtClustDB; PRK05294; -.
DR   BioCyc; PSP312153:PNUC_1018-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; IPR005479; CarbamoylP_synth_lsu_ATP-bd.
DR   InterPro; IPR005483; CarbamoylP_synth_lsu_CPS-dom.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 2.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:1.10.1030.10; CarbamoylP_synth_lsu_oligo; 1.
DR   Gene3D; G3DSA:3.40.50.1380; MGS-like_dom; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 2.
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; 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; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   HOGENOMDNA; POLSQ_1.PE1012; -.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
SQ   SEQUENCE   1087 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKRSDIKSI LIIGAGPIVI GQACEFDYSG AQACKALRDE GYKVILVNSN PATIMTDPEM
     ADVTYIEPIT WEVVERIIAA EKPDAILPTM GGQTALNCAL DLHRHGVLEK YGCELIGASP
     EAIDKAEDRQ KFKNAMTKIG LGSAKSGIAH SMDEAHEVQQ HIQQETGSSG FPVVIRPSFT
     MGGSGGGIAY NREEFEEICK RGLDLSPTRE LLIEESLLGW KEFEMEVVRD RNDNCIIVCS
     IENLDPMGVH TGDSITVAPA QTLTDKEYQI MRNASIAVLR EIGVDTGGSN VQFSINPVDG
     RMIVIEMNPR VSRSSALASK ATGFPIAKIA AKLAVGYTLD ELKNDITGGA TPASFEPSID
     YVVTKIPRFA FEKFPQADSR LTTQMKSVGE VMAIGRTFQE SFQKALRGLE VGVDGLDEVS
     TDLDDIIQEI NEPGPDRIWY LADAFRMGMG LDEIYSETKV DPWFLEQIEE LITIETELKQ
     RKIDSLSAPE LRAVKQKGFS DRRLAKLLGV DASSVRAARH RLKVVPVYKR VDTCAAEFST
     NTAYMYSTYE AEHGECESRP TNKDKIMVLG GGPNRIGQGI EFDYCCVHAA LAMRDDGYET
     IMVNCNPETV STDYDTSDRL YFEPLTLEDV LEIVAKEKPK GVIVQYGGQT PLKLALDLER
     NGVPIIGTSP DMIDAAEDRE RFQKLLQDLG LRQPPNRTAR TEEEALKLAE EIGYPLVVRP
     SYVLGGRAME IVHDGRDLER YMREAVKVSH DSPVLLDRFL NDAIECDVDC ISDGTKVFIG
     GVMEHIEQAG VHSGDSACSL PPYSLSDATV EEIKRQTAAM AKGLHVIGLM NVQFAIQNVD
     GQDVIYVLEV NPRASRTVPF VSKATGLQLA KIAARCMVGQ TLEQQGIQAE VKPPYFSVKE
     AVFPFNKFPG IDPILGPEMR STGEVMGVGK TFGEALFKSQ LGAGIKLPKS GTVLLTVKDS
     DKPKAVEVAK LLHQLGFPMV ATKGTAAAIE AAGLPVKLVN KVKDGRPHIV DFIKNGEISL
     VFTTVDETRT AIADSRSIRT SAQANGVTYY TTISAARAVM DGLLASQNGS KESLEVYSLQ
     NLHRTLI
//

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