ID A0A1V9Y5B1_9STRA Unreviewed; 437 AA.
AC A0A1V9Y5B1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000256|ARBA:ARBA00012075, ECO:0000256|RuleBase:RU000598};
DE EC=4.2.1.19 {ECO:0000256|ARBA:ARBA00012075, ECO:0000256|RuleBase:RU000598};
GN ORFNames=ACHHYP_17046 {ECO:0000313|EMBL:OQR80915.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR80915.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR80915.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR80915.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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|ARBA:ARBA00001723,
CC ECO:0000256|RuleBase:RU000598};
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|RuleBase:RU000598}.
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000256|ARBA:ARBA00007481, ECO:0000256|RuleBase:RU000598}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR80915.1}.
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DR EMBL; JNBR01002859; OQR80915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9Y5B1; -.
DR STRING; 1202772.A0A1V9Y5B1; -.
DR OrthoDB; 36911at2759; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR006438; HAD-SF_TIGR01548.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006543; Histidinol-phos.
DR InterPro; IPR038494; IGPD_sf.
DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR NCBIfam; TIGR01548; HAD-SF-IA-hyp1; 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; PF00702; Hydrolase; 1.
DR Pfam; PF00475; IGPD; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW ECO:0000256|RuleBase:RU000598};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000598};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000243579}.
SQ SEQUENCE 437 AA; 46408 MW; 6D01E47370CA08ED CRC64;
MQALLWDMDG VLAEVSRSYR AAIVATAAAF GATVTDDDVE VAKLAGDANN DWVLTHKLVH
NKVAGASATL AEITAKFEEI YQGTASAPGL CSLETLITAK GLLVELNRRL PKGMAIVTGR
PKKDCDKFLA DHGLEPLFPV RVCMEDGPPK PSPAPILLAL QRLNVPASQV AMIGDTVDDI
TAAVRASVLA YGVITPGAYA NAVLQYTTAP IVTKLLSVGA KRVLRPGCDE LLDEIPVTAV
AAGERRGKIH RQTKETSIHV DLDLDGNGTS DISTGIGFLD HMLDAVAKHG RFNLVLKCKG
DTWIDDHHTT EDCGLALGEA FDMALGPRKD IARFGSALVP LDEALSRVIV DISSRGCSAV
AMDLRRPSIG TLSTEMIPHF FVSFASAARL TLHVDVVKGE NDHHKAEASF KAFARALRQA
VALDPTAGVP STKGMLA
//
