ID D0J912_BLASP Unreviewed; 378 AA.
AC D0J912;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_00076};
DE Short=IGPD {ECO:0000256|HAMAP-Rule:MF_00076};
DE EC=4.2.1.19 {ECO:0000256|HAMAP-Rule:MF_00076};
GN Name=hisB {ECO:0000256|HAMAP-Rule:MF_00076,
GN ECO:0000313|EMBL:ACX83833.1};
GN OrderedLocusNames=BPLAN_204 {ECO:0000313|EMBL:ACX83833.1};
OS Blattabacterium sp. subsp. Periplaneta americana (strain BPLAN)
OS (Periplaneta americana symbiotic bacterium).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=600809 {ECO:0000313|EMBL:ACX83833.1, ECO:0000313|Proteomes:UP000002225};
RN [1] {ECO:0000313|EMBL:ACX83833.1, ECO:0000313|Proteomes:UP000002225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPLAN {ECO:0000313|EMBL:ACX83833.1,
RC ECO:0000313|Proteomes:UP000002225};
RX PubMed=19880743; DOI=10.1073/pnas.0907504106;
RA Sabree Z.L., Kambhampati S., Moran N.A.;
RT "Nitrogen recycling and nutritional provisioning by Blattabacterium, the
RT cockroach endosymbiont.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19521-19526(2009).
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:0000256|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:0000256|ARBA:ARBA00005047, ECO:0000256|HAMAP-Rule:MF_00076}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00076}.
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000256|HAMAP-Rule:MF_00076}.
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DR EMBL; CP001429; ACX83833.1; -; Genomic_DNA.
DR RefSeq; WP_012821361.1; NC_013418.2.
DR AlphaFoldDB; D0J912; -.
DR STRING; 600809.BPLAN_204; -.
DR KEGG; bpi:BPLAN_204; -.
DR eggNOG; COG0131; Bacteria.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_044308_0_0_10; -.
DR OrthoDB; 9790411at2; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000002225; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:InterPro.
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 Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR HAMAP; MF_00076; HisB; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005954; HisB_N.
DR InterPro; IPR006543; Histidinol-phos.
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 NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR NCBIfam; TIGR01261; hisB_Nterm; 1.
DR NCBIfam; TIGR01656; Histidinol-ppas; 1.
DR PANTHER; PTHR23133:SF2; IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE; 1.
DR PANTHER; PTHR23133; IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR Pfam; PF00475; IGPD; 1.
DR SUPFAM; SSF56784; HAD-like; 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00076};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00076};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_00076};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00076};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000002225}.
SQ SEQUENCE 378 AA; 43579 MW; 6003A4E0654CF543 CRC64;
MKRILFIDRD GTIIQEFPPT YQIDSLEKVN FYPRVLFFLT KIAHELNYDF VMVTNQDGLG
TDKFPEKNFW PIHNHILKIL KTEGIHFSSV HIDRTFPEEN SPTRKPGIGM LTSYFHSGYN
LEKSFVIGDR LTDVLLAKNL GCKSIWINPI IEEKNLSIEK KSLKKIIALE TDSWERIYEY
LKDVSTKRIF QHQRKTLETD VKITIQLYGE GKAKIQTGLG FLDHLLEQMA FHSLMDLNIH
AIGDLEVDEH HTIEDTAITL GEIFHQSIID KRGIERYGFF SLPMDDCLAT VALDLGGRSQ
LTWKAKFIRN KIGKVPTEMF IHFFKSFSSS AKCNLYVHAI GKNDHHKIES IFKAFAKAIK
MAIKKNRTNK LPSSKGML
//
