ID   HIS7_AROAE              Reviewed;         195 AA.
AC   Q5P792;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_00076};
DE            Short=IGPD {ECO:0000255|HAMAP-Rule:MF_00076};
DE            EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_00076};
GN   Name=hisB {ECO:0000255|HAMAP-Rule:MF_00076}; OrderedLocusNames=AZOSEA06960;
GN   ORFNames=ebA1296;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-
CC         4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00076};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC       {ECO:0000255|HAMAP-Rule:MF_00076}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00076}.
CC   -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00076}.
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DR   EMBL; CR555306; CAI06819.1; -; Genomic_DNA.
DR   RefSeq; WP_011236547.1; NC_006513.1.
DR   AlphaFoldDB; Q5P792; -.
DR   SMR; Q5P792; -.
DR   STRING; 76114.ebA1296; -.
DR   KEGG; eba:ebA1296; -.
DR   eggNOG; COG0131; Bacteria.
DR   HOGENOM; CLU_044308_2_0_4; -.
DR   OrthoDB; 9790411at2; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000006552; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07914; IGPD; 1.
DR   HAMAP; MF_00076; HisB; 1.
DR   InterPro; IPR038494; IGPD_sf.
DR   InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR   InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR23133:SF2; IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE; 1.
DR   PANTHER; PTHR23133; IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7; 1.
DR   Pfam; PF00475; IGPD; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR   PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR   PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..195
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /id="PRO_0000336296"
SQ   SEQUENCE   195 AA;  21486 MW;  51D6D81BBA7D09C1 CRC64;
     MRQAEVTRDT LETRITARVD LDGSGKAAFA TGVPFLDHML DQIARHGAFD LDIRAEGDTH
     IDDHHTVEDV GITLGQAFAR ALGDKRGIRR YGHAYVPLDE ALSRVVVDFS GRPGLHYFVS
     YTRARIGSFD VDLAREFFQG FVNHAGVTLH IDSLRGDNAH HQCETIFKAF GRALRMAAER
     DERAAGAIPS TKGAL
//