(data stored in ACNUC7421 zone)

HOGENOM: DEHSB_1_PE1000

ID   DEHSB_1_PE1000                       STANDARD;      PRT;   1079 AA.
AC   DEHSB_1_PE1000; A5FQD1;
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; (DEHSB_1.PE1000).
GN   Name=carB; OrderedLocusNames=DehaBAV1_1012;
OS   DEHALOCOCCOIDES SP. BAV1.
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=216389;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEHSB_1.PE1000.
CC       Dehalococcoides sp. BAV1, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:A5FQD1_DEHSB
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: HOG000234583 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A5FQD1; -.
DR   EMBL; CP000688; ABQ17592.1; -; Genomic_DNA.
DR   RefSeq; YP_001214470.1; NC_009455.1.
DR   ProteinModelPortal; A5FQD1; -.
DR   STRING; A5FQD1; -.
DR   GeneID; 5131959; -.
DR   GenomeReviews; CP000688_GR; DehaBAV1_1012.
DR   KEGG; deb:DehaBAV1_1012; -.
DR   eggNOG; COG0458; -.
DR   OMA; QGVTKEI; -.
DR   ProtClustDB; CLSK837072; -.
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; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   HOGENOMDNA; DEHSB_1.PE1000; -.
KW   carbamoyl-phosphate synthase large subunit;
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   1079 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNKPKKVLII GSGPIIIGQA AEFDYAGTQA CKAMREEGVE SILVNSNPAT IMTDENVADR
     VYIEPLTVES ITKIIEKERP DGLLPTLGGQ TGLNLAVDLA DAGVLAKYNV RSLGTPINTI
     RTAEDRELFK ELLTKIGEPV PPSETVTTAE DALRVAHMIG LPVVIRPAYT LGGTGGGFAH
     NWDEVEEVAQ TGLNASPIHQ ILVEKSVAGW KEIEYEVMRD GADNCITICN MENFDPMGVH
     TGDSIVVVPV QTLTNKESQM LRTASIKIIR ALGIEGGCNV QLSLNPNGNE YYVIEVNPRV
     SRSSALASKA TGYPIARVAS KIAIGKRLDE IPNAVTGKTL ACFEPAVDYI VAKIPRFPFD
     KFALGDRGLG TQMKATGEVM AIDRSFEAAI HKSIRSLEFG KKTVLWEDRS WIMGDDLSTY
     PLHAHDTRLW TILAALRRGH TPEAIHEKTM VDNWFLYKLK NITNMEKRLL KENLTPLLML
     EAKQMGFSDE EIATLSGKLA EQVRQTRLEW NIKPVFKMVD TCAAEFDAAT PYFYSTYDDE
     NEAIPQNVKK AVVIGSGPIR IGQGIEFDYC SVHAAWALEK AGLQSIMINS NPETVSTDFD
     TSNRLYFEAL DEESVRDILE NENISAPEST PSIVQFGGQT AINLAAPLTR SSNPIIGSSA
     EAIDLAEDRR RFERLLSEMG IPQAPGAGIT SLDEALSIAD SIGYPVVVRP SYVLGGRAME
     IVSDASDLVR YMSAAIELNT GHPILIDKYL VGKEVEVDAI ADGETVFIPG VMEHIERAGV
     HSGDSMAVYP TQNLNEHDLA TITDYTIRIG KALNVRGLMN IQFVVSKDPE GGDNIVYVLE
     VNPRGSRTVP FLSKVTGVPM VDIAVNVMLG KTINEQGYQN GIMPNTDLVA IKAPVFSMAK
     LVGVDTYLGP EMKSTGEVMG VDHTFNKALV KTLQAASIML PETGTLLFSI ADRDKAEALP
     LIRTLHGLGY NFYATEGTAA MITAAGITVK QISKKLDEGH PNIVDIIRNG TVCGVINTMT
     GGRVPLRDGF YIRRAAAERK VPCFTSMDTA KAAVEALANG NRQITVLPLN EYRQGKSGS
//

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