ID   HIS5_AZOBR     STANDARD;      PRT;   192 AA.
AC   P18785;
DT   01-NOV-1990 (Rel. 16, Created)
DT   01-AUG-1992 (Rel. 23, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Imidazole glycerol phosphate synthase subunit hisH (EC 2.4.2.-) (IGP
DE   synthase glutamine amidotransferase subunit) (IGP synthase subunit
DE   hisH) (ImGP synthase subunit hisH) (IGPS subunit hisH).
GN   Name=hisH;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sp6;
RX   MEDLINE=89313660; PubMed=2664449;
RA   Fani R., Bazzicalupo M., Damiani G., Bianchi A., Schipani C.,
RA   Sgaramella V., Polsinelli M.;
RT   "Cloning of histidine genes of Azospirillum brasilense: organization
RT   of the ABFH gene cluster and nucleotide sequence of the hisB gene.";
RL   Mol. Gen. Genet. 216:224-229(1989).
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 PRPP: step 5.
CC   -!- SUBUNIT: Heterodimer of hisH and hisF (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity).
CC   -!- SIMILARITY: Contains 1 type-1 glutamine amidotransferase domain.
CC   -!- CAUTION: Compared to other hisH it lacks an internal segment that
CC       normally contains the Cys active site residue.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X17435; CAA35479.1; -.
DR   EMBL; X61207; CAA43516.1; -.
DR   PIR; S16799; PE0007.
DR   HSSP; Q9X0C8; 1GPW.
DR   HAMAP; MF_00278; atypical; 1.
DR   InterPro; IPR000991; GATase_1.
DR   InterPro; IPR010139; IMP_synth_hisH.
DR   Pfam; PF00117; GATase; 1.
DR   TIGRFAMs; TIGR01855; IMP_synth_hisH; 1.
DR   PROSITE; PS00442; GATASE_TYPE_I; FALSE_NEG.
KW   Glutamine amidotransferase; Histidine biosynthesis; Transferase.
FT   ACT_SITE    172    172       By similarity.
FT   ACT_SITE    174    174       By similarity.
SQ   SEQUENCE   192 AA;  20826 MW;  AB07AB18A14257B9 CRC64;
     METVALIDYG SGNLRSPAKA LERAAAGCHA SFQVLVTSDA DAVRKADRVV LPAVGAFADC
     KRGLSEVPGM QLMAEGGREY GVTEGLGWIK GEVVKLEPAD PTLKIPHMGW NELDIRREHP
     VLAGLRERAH AYFVHSYRFA VERPEDVIAS ADYGGPFAAV VGRDNLVGTQ FHPEKSQETG
     LALVANFLTW RV
//