(data stored in ACNUC9435 zone)

HOGENOM: NOVAD_1_PE1003

ID   NOVAD_1_PE1003                       STANDARD;      PRT;   209 AA.
AC   NOVAD_1_PE1003; Q2G9M1;
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   SubName: Full=Imidazole glycerol phosphate synthase subunit hisH;
DE   EC=2.4.2 -; (NOVAD_1.PE1003).
GN   OrderedLocusNames=Saro_1007;
OS   NOVOSPHINGOBIUM AROMATICIVORANS DSM 12444.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NOVAD_1.PE1003.
CC       Novosphingobium aromaticivorans DSM 12444, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:Q2G9M1_NOVAD
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to
CC       IGP, AICAR and glutamate. The hisH subunit provides the glutamine
CC       amidotransferase activity that produces the ammonia necessary to
CC       hisF for the synthesis of IGP and AICAR (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1-
CC       ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-
CC       carboxamide + L-glutamine = imidazole-glycerol phosphate + 5-
CC       aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC   -!- SUBUNIT: Heterodimer of hisH and hisF (By similarity).
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   -!- GENE_FAMILY: HOG000025030 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q2G9M1; -.
DR   EMBL; CP000248; ABD25452.1; -; Genomic_DNA.
DR   RefSeq; YP_496286.1; NC_007794.1.
DR   ProteinModelPortal; Q2G9M1; -.
DR   STRING; Q2G9M1; -.
DR   GeneID; 3915789; -.
DR   GenomeReviews; CP000248_GR; Saro_1007.
DR   KEGG; nar:Saro_1007; -.
DR   NMPDR; fig|48935.1.peg.3111; -.
DR   eggNOG; COG0118; -.
DR   OMA; WNEINIV; -.
DR   ProtClustDB; PRK13146; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00278; HisH; 1; -.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR010139; Imidazole-glycPsynth_HisH.
DR   Pfam; PF00117; GATase; 1.
DR   PIRSF; PIRSF000495; Amidotransf_hisH; 1.
DR   TIGRFAMs; TIGR01855; IMP_synth_hisH; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   HOGENOMDNA; NOVAD_1.PE1003; -.
KW   Amino-acid biosynthesis; Complete proteome;
KW   Glutamine amidotransferase; Glycosyltransferase;
KW   Histidine biosynthesis; Transferase.
SQ   SEQUENCE   209 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAETLALVDY GAGNLRSVAN ALKAAGAEGV VVTADPAVVR AADRVVLPGV GAFKACIGAL
     RGVSGLVEAM EERVLVGGAP FLGICVGMQL LADRGVEHGV TEGLGWIGGE VRVIEPADPS
     IKVPHMGWND VAPMPHEGGA ELIEPGEAYF LHSYHFVTDA GAHIAAMSDH GGGIVAAVAR
     DNILGVQFHP EKSQSYGLSL LARFLEWKP
//

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