ID D5BA27_ZUNPS Unreviewed; 251 AA.
AC D5BA27;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 01-MAY-2013, entry version 23.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF;
DE EC=4.1.3.-;
DE AltName: Full=IGP synthase cyclase subunit;
DE AltName: Full=IGP synthase subunit HisF;
DE AltName: Full=ImGP synthase subunit HisF;
GN Name=hisF; OrderedLocusNames=ZPR_2000;
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87;
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B.,
RA Dang H.Y., Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its
RT adaptation to the deep-sea environment and ecological role in
RT sedimentary organic nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to
CC IGP, AICAR and glutamate. The HisF subunit catalyzes the
CC cyclization activity that produces IGP and AICAR from PRFAR using
CC the ammonia provided by the HisH subunit (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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
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DR EMBL; CP001650; ADF52325.1; -; Genomic_DNA.
DR RefSeq; YP_003584521.1; NC_014041.1.
DR ProteinModelPortal; D5BA27; -.
DR EnsemblBacteria; ADF52325; ADF52325; ZPR_2000.
DR GeneID; 9077872; -.
DR KEGG; zpr:ZPR_2000; -.
DR PATRIC; 37233401; VBIZunPro130839_1918.
DR HOGENOM; HOG000224612; -.
DR KO; K02500; -.
DR OMA; RVVKGTN; -.
DR UniPathway; UPA00031; UER00010.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:HAMAP.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01013; HisF; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR004651; HisF.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; RibP_bind_barrel; 1.
DR TIGRFAMs; TIGR00735; hisF; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW Histidine biosynthesis; Lyase.
FT ACT_SITE 11 11 By similarity.
FT ACT_SITE 130 130 By similarity.
SQ SEQUENCE 251 AA; 27208 MW; 241A86A8CC656D22 CRC64;
MLTKRIIPCL DIKNGRTVKG VNFVDLRDAG DPVELASKYA ETGADELVFL DISATEERRK
TLANLVLRVA EKVNIPFTVG GGISSIEDVD ILLKNGADKV SVNSSAVKNP DLINELSQKF
GAQCITVAID AKQINGQWIV HLVGGKVPTE LDLFEWAKEV EQRGAGEILF TSMNNDGTKD
GFANIALKKL SEDLNIPIIA SGGAGNIQHF VDTFKEGKAD AALAASVFHF KEIEIPELKK
ELKKQGIPVR I
//
