HIS7_CERS4
ID HIS7_CERS4 Reviewed; 195 AA.
AC O33564; Q3J483;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 115.
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}; Synonyms=hisBD;
GN OrderedLocusNames=RHOS4_08330; ORFNames=RSP_2246;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Oriol E., Barbe J., Gibert I.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; X87256; CAA60712.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA78401.1; -; Genomic_DNA.
DR RefSeq; WP_009566359.1; NZ_CP030271.1.
DR RefSeq; YP_352302.1; NC_007493.2.
DR AlphaFoldDB; O33564; -.
DR SMR; O33564; -.
DR STRING; 272943.RSP_2246; -.
DR EnsemblBacteria; ABA78401; ABA78401; RSP_2246.
DR GeneID; 67446018; -.
DR KEGG; rsp:RSP_2246; -.
DR PATRIC; fig|272943.9.peg.1149; -.
DR eggNOG; COG0131; Bacteria.
DR OMA; ARHGLFD; -.
DR PhylomeDB; O33564; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000002703; Chromosome 1.
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 Gene3D; 3.30.230.40; -; 2.
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_S5_D2-typ_fold.
DR PANTHER; PTHR23133; PTHR23133; 1.
DR Pfam; PF00475; IGPD; 1.
DR SUPFAM; SSF54211; SSF54211; 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_0000158164"
FT CONFLICT 43..52
FT /note="LARHALIDIT -> ARPARADRHP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..87
FT /note="RG -> AR (in Ref. 1; CAA60712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 21565 MW; A428EC47E3D79B0E CRC64;
MRKAEISRKT AETDISVTVD LDGTGRYDIR TGVGFFDHMM DQLARHALID ITLRCEGDLH
IDDHHTVEDC GIALGQALTR ALGDKRGIRR YGSFHLAMDD ALVRAALDLS GRPFLVWNLP
FPTEKIGSFD TELVREFFQA LATHGGITLH VDLIHGVNSH HIAEAAFKAV ARSLREAVEP
DPRRADAIPS TKGML