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Database: UniProt
Entry: A0A172TRX6_9BACT
LinkDB: A0A172TRX6_9BACT
Original site: A0A172TRX6_9BACT 
ID   A0A172TRX6_9BACT        Unreviewed;       387 AA.
AC   A0A172TRX6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000256|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Histidinol-phosphatase {ECO:0000256|HAMAP-Rule:MF_01022};
DE              EC=3.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_01022};
DE              Short=IGPD {ECO:0000256|HAMAP-Rule:MF_01022};
DE              EC=4.2.1.19 {ECO:0000256|HAMAP-Rule:MF_01022};
GN   Name=hisB {ECO:0000256|HAMAP-Rule:MF_01022};
GN   ORFNames=SY85_04345 {ECO:0000313|EMBL:ANE49835.1};
OS   Flavisolibacter tropicus.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavisolibacter.
OX   NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE49835.1, ECO:0000313|Proteomes:UP000077177};
RN   [1] {ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANE49835.1, ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|EMBL:ANE49835.1,
RC   ECO:0000313|Proteomes:UP000077177};
RX   PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA   Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA   Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT   "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL   Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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_01022};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC         Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01022};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01022};
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_01022}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       imidazoleglycerol-phosphate dehydratase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01022}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC       phosphatase family. {ECO:0000256|HAMAP-Rule:MF_01022}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01022}.
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DR   EMBL; CP011390; ANE49835.1; -; Genomic_DNA.
DR   RefSeq; WP_066401975.1; NZ_CP011390.1.
DR   AlphaFoldDB; A0A172TRX6; -.
DR   STRING; 1492898.SY85_04345; -.
DR   KEGG; fla:SY85_04345; -.
DR   PATRIC; fig|1492898.3.peg.950; -.
DR   OrthoDB; 9790411at2; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000077177; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_01022; Bifunc_HisB; 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; IPR020566; His_synth_bifunc_HisB.
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_01022};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01022};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01022};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01022, ECO:0000313|EMBL:ANE49835.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01022};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01022};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01022};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01022}; Reference proteome {ECO:0000313|Proteomes:UP000077177}.
FT   REGION          1..196
FT                   /note="Histidinol-phosphatase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   REGION          197..387
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   ACT_SITE        16
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   ACT_SITE        18
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
SQ   SEQUENCE   387 AA;  43571 MW;  486CE0263CF4F27B CRC64;
     MAANTTTQGK RVLFIDRDGT LIQECPPTYQ IDSFDKVSFY PQVFKYMIKI AEELDYELVM
     VSNQDGLGTA SFPEADFWPV HNLVMSSFAN EGVIFKEELI DRSFPEDNLP TRKPGVGMFT
     KYLNNPEYDI ANSFVIGDRI TDVQLAKNLK CKAIWLKNNP ELGAAEVSDD AKALEEVVVL
     ATEHWRDIYE YLKLGKREVG HIRITNETNI AVGLNLDGSG KASIDTGLGF FDHMLDQIAR
     HGLIDLSVHS KGDLHIDEHH TVEDTGIALG EAFAKAIGDK KGIERYGFAL PMDEAEAKVL
     LDFGGRNWLV WNTHFSRERV GDVPTEMFYH FFKSFSDAAK CNLNIECRGE NEHHKIEAIF
     KAFAKAIKMA VKRDPLKNYL PSTKGVL
//
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