HIS7_NITHX
ID HIS7_NITHX Reviewed; 197 AA.
AC Q1QRX4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Nham_0122;
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG US DOE Joint Genome Institute;
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., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) 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; CP000319; ABE61023.1; -; Genomic_DNA.
DR RefSeq; WP_011508730.1; NC_007964.1.
DR AlphaFoldDB; Q1QRX4; -.
DR SMR; Q1QRX4; -.
DR STRING; 323097.Nham_0122; -.
DR EnsemblBacteria; ABE61023; ABE61023; Nham_0122.
DR KEGG; nha:Nham_0122; -.
DR eggNOG; COG0131; Bacteria.
DR HOGENOM; CLU_044308_3_0_5; -.
DR OMA; ARHGLFD; -.
DR OrthoDB; 1278103at2; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000001953; 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 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..197
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_1000010310"
SQ SEQUENCE 197 AA; 21374 MW; E18D9E67E347FE8E CRC64;
MRTATIKRKT KETDIEVAVN LDGSGVSSVA TGIGFFDHML DLLARHSRID IMVKADGDLH
VDYHHTTEDV GIALGQAVKQ ALGTMAGITR YACAHMPMDE TLSRVVIDIS GRPMLVFKVE
FPRDKIGEFD TELVREWFNA FAVNAGVTLH VETLYGENSH HIAESCFKGL ARALRAAVAI
DPRAAGEVPS TKGQLGG
