HIS7_SPILD
ID HIS7_SPILD Reviewed; 382 AA.
AC D2QPE6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000255|HAMAP-Rule:MF_01022};
DE Includes:
DE RecName: Full=Histidinol-phosphatase {ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000303|PubMed:25848029};
DE EC=3.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:25848029};
DE Includes:
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000250|UniProtKB:P06987, ECO:0000255|HAMAP-Rule:MF_01022};
DE Short=IGPD {ECO:0000250|UniProtKB:P06987, ECO:0000255|HAMAP-Rule:MF_01022};
DE EC=4.2.1.19 {ECO:0000250|UniProtKB:P06987, ECO:0000255|HAMAP-Rule:MF_01022};
GN Name=hisB {ECO:0000250|UniProtKB:P06987, ECO:0000255|HAMAP-Rule:MF_01022};
GN OrderedLocusNames=Slin_3446 {ECO:0000312|EMBL:ADB39454.1};
OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Spirosoma.
OX NCBI_TaxID=504472 {ECO:0000312|Proteomes:UP000002028};
RN [1] {ECO:0000312|Proteomes:UP000002028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896 {ECO:0000312|Proteomes:UP000002028};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S.,
RA Goker M., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Spirosoma linguale DSM 74.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
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_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:0000255|HAMAP-Rule:MF_01022,
CC ECO:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01022,
CC ECO:0000269|PubMed:25848029};
CC Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:Q9S5G5};
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_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:0000255|HAMAP-Rule:MF_01022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01022}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC phosphatase family. {ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC imidazoleglycerol-phosphate dehydratase family. {ECO:0000255|HAMAP-
CC Rule:MF_01022, ECO:0000305}.
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DR EMBL; CP001769; ADB39454.1; -; Genomic_DNA.
DR AlphaFoldDB; D2QPE6; -.
DR SMR; D2QPE6; -.
DR STRING; 504472.Slin_3446; -.
DR EnsemblBacteria; ADB39454; ADB39454; Slin_3446.
DR KEGG; sli:Slin_3446; -.
DR eggNOG; COG0131; Bacteria.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_044308_0_0_10; -.
DR OMA; PEDTFWP; -.
DR UniPathway; UPA00031; UER00011.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000002028; 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; 3.30.230.40; -; 2.
DR Gene3D; 3.40.50.1000; -; 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; IPR013954; PNK3P.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR23133; PTHR23133; 1.
DR Pfam; PF00475; IGPD; 1.
DR Pfam; PF08645; PNK3P; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR TIGRFAMs; TIGR01261; hisB_Nterm; 1.
DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Hydrolase;
KW Lyase; Magnesium; Metal-binding; Multifunctional enzyme.
FT CHAIN 1..382
FT /note="Histidine biosynthesis bifunctional protein HisB"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435610"
FT REGION 1..190
FT /note="Histidinol-phosphatase"
FT /evidence="ECO:0000250|UniProtKB:P06987, ECO:0000255|HAMAP-
FT Rule:MF_01022"
FT REGION 191..382
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /evidence="ECO:0000250|UniProtKB:P06987, ECO:0000255|HAMAP-
FT Rule:MF_01022"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000305"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000305"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9S5G5, ECO:0000255|HAMAP-
FT Rule:MF_01022"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9S5G5, ECO:0000255|HAMAP-
FT Rule:MF_01022"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9S5G5, ECO:0000255|HAMAP-
FT Rule:MF_01022"
SQ SEQUENCE 382 AA; 42684 MW; 25F741A188DA7894 CRC64;
MQKIVFIDRD GTLIAEPQPD QQVDSLAKLD FIPKAISAMR KIAEDTTYEL VMVTNQDGLG
TGSFPEDTFW PAHNKMMSTF AGENVNFAAV HIDRHFPHDN SSTRKPGVGM LTQYFEASYD
LTNSFVIGDR LTDVQLAVNL GAKAILFMPP NGLAAVQSAD VSGLTEAMKQ AIVLQTGDWD
EIYEFLRLPA RTALVERNTK ETQIRVELNL DGRGRADMHT GLGFFDHMLD QVAKHSGADL
AIHVNGDLHI DEHHTIEDTA LALGEAYRRA LGDKRGISRY GFLLPMDEAL AQVGIDFSGR
PWLVWDAEFK REKIGDMPTE MFYHFFKSFS DTALCNLNIK VEGDNEHHKI EAIFKAFAKA
IKMAVRRDIN ELDNLPSTKG VL
