(data stored in ACNUC7421 zone)

HOGENOM: SHESW_1_PE1000

ID   SHESW_1_PE1000                       STANDARD;      PRT;   1074 AA.
AC   SHESW_1_PE1000; A1RGQ8;
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;Flags:
DE   Precursor; (SHESW_1.PE1000).
GN   Name=carB; OrderedLocusNames=Sputw3181_1003;
OS   SHEWANELLA SP. W3-18-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHESW_1.PE1000.
CC       Shewanella sp. W3-18-1, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:A1RGQ8_SHESW
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; A1RGQ8; -.
DR   EMBL; CP000503; ABM23853.1; -; Genomic_DNA.
DR   RefSeq; YP_962407.1; NC_008750.1.
DR   ProteinModelPortal; A1RGQ8; -.
DR   STRING; A1RGQ8; -.
DR   GeneID; 4659915; -.
DR   GenomeReviews; CP000503_GR; Sputw3181_1003.
DR   KEGG; shw:Sputw3181_1003; -.
DR   eggNOG; COG0458; -.
DR   OMA; QGVTKEI; -.
DR   ProtClustDB; PRK05294; -.
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; SHESW_1.PE1000; -.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat; Signal.
SQ   SEQUENCE   1074 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM
     ADATYIEPIH WEVVRNIIAK ERPDAILPTM GGQTALNCAL ELEAKGVLAE FNVEMIGATA
     DAIDKAEDRS RFDKAMKSIG LECPRAGIAH SMEEAYGVLE QVGFPCIIRP SFTMGGSGGG
     IAYNKEEFEE ICSQGLDLSP TKELLIDESL IGWKEYEMEV VRDRNDNCII VCSIENFDPM
     GVHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFGINP IDGRMVIIEM
     NPRVSRSSAL ASKATGFPIA KIAAKLAVGF TLDELMNDIT GGRTPASFEP AIDYVVTKVP
     RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT FQESLQKALR GLEVSRNGLD PITDMSKPEA
     MSRIRLELKE PGCDRIWYIA DAMRAGLGLD EIFRLTNIDP WFLVQIEELI KLEGVVAEAG
     LAGLDYDLLR KLKRKGFADA RLADVLGVNE AEVRKLRDKF DLHPVYKRVD TCAAEFATDT
     AYMYSTYEEE CEANPSDREK IMVLGGGPNR IGQGIEFDYC CVHAALALRE DGYETIMVNC
     NPETVSTDYD TSDRLYFEPV TLEDVLEIVR IEKPKGVIVQ YGGQTPLKLA RALEAAGVPI
     IGTSPDAIDR AEDRERFQQA IQRLEMKQPE NDTVTTVEGA VIAAERIGYP LVVRPSYVLG
     GRAMEIVYDQ QDLLRYFNEA VSVSNASPVL LDHFLDDAIE VDIDAVCDGE TVVIGAIMEH
     IEQAGVHSGD SGCSLPPYTL SQEIQDRMRV QVGKLAMELG VVGLMNVQFA VKDNEIYMIE
     VNPRAARTVP FVSKATGVPL AKIAARVMAG QSLKSQNFTK EVIPPFYSVK EVVLPFNKFP
     GVDPLLGPEM RSTGEVMGVG DTFAEAYAKA QLGATAEVPK SGRALLSVRN SDKKRVADLA
     AKLIELGYQI DATHGTAIIL GEAGINPRLV NKVHEGRPHI LDRIKNGEYT YIVNTTEGRQ
     AIEDSRQLRR GALRYKVNYT TTMNAAFATC MAHAADDRTN VTSVQELHQR VLAE
//

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