ID HIS7_CALS8 Reviewed; 194 AA.
AC A4XL23;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 38.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase;
DE Short=IGPD;
DE EC=4.2.1.19;
GN Name=hisB; OrderedLocusNames=Csac_2023;
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis;
OC Caldicellulosiruptor.
OX NCBI_TaxID=351627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L.,
RA Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M.,
RA Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W.,
RA Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3-
CC phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family.
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DR EMBL; CP000679; ABP67608.1; -; Genomic_DNA.
DR RefSeq; YP_001180799.1; NC_009437.1.
DR ProteinModelPortal; A4XL23; -.
DR STRING; 351627.Csac_2023; -.
DR EnsemblBacteria; ABP67608; ABP67608; Csac_2023.
DR GeneID; 5088763; -.
DR KEGG; csc:Csac_2023; -.
DR PATRIC; 21253790; VBICalSac56748_2201.
DR eggNOG; COG0131; -.
DR HOGENOM; HOG000228064; -.
DR KO; K01693; -.
DR OMA; HHIVEAC; -.
DR ProtClustDB; CLSK2473404; -.
DR BioCyc; CSAC351627:GJ17-2064-MONOMER; -.
DR UniPathway; UPA00031; UER00011.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:HAMAP.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00076; HisB; 1; -.
DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR23133:SF2; PTHR23133:SF2; 1.
DR Pfam; PF00475; IGPD; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 2.
DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW Histidine biosynthesis; Lyase.
FT CHAIN 1 194 Imidazoleglycerol-phosphate dehydratase.
FT /FTId=PRO_0000336298.
SQ SEQUENCE 194 AA; 21796 MW; CB01964B078F67FE CRC64;
MNARIAEVQR KTKETEIKMV LNIDGDGEYK ISTGIGFFDH MLQLFCHHGK FNIQVEAKGD
LHIDDHHTIE DVGIVLGQAF LKAISDKRGI KRYSHIILPM DEALIMVAID ISGRPYLAFD
VDFRLPKLGE MNSQMVVEFF RAFVSSAKVT LHVKKISGEN DHHVCEAIFK AFGRVLKDAC
TIVDDKIPSS KGVL
//
