HIS7_MYCTU
ID HIS7_MYCTU Reviewed; 210 AA.
AC P9WML9; L0T8R8; O06590; P64368;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
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, ECO:0000269|PubMed:24311587};
GN Name=hisB {ECO:0000255|HAMAP-Rule:MF_00076}; OrderedLocusNames=Rv1601;
GN ORFNames=MTCY336.03c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 2-210 IN COMPLEX WITH MANGANESE;
RP SUBSTRATE AND ATZ, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=24311587; DOI=10.1107/s0907444913022579;
RA Ahangar M.S., Vyas R., Nasir N., Biswal B.K.;
RT "Structures of native, substrate-bound and inhibited forms of Mycobacterium
RT tuberculosis imidazoleglycerol-phosphate dehydratase.";
RL Acta Crystallogr. D 69:2461-2467(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-210.
RA Kumar D., Jha B., Ahangar M.S., Kumar B.B.;
RT "Crystal structure of Mycobacterium tuberculosis HisB bound with an
RT inhibitor.";
RL Submitted (MAR-2017) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RA Kumar D., Pal R.K., Biswal B.K.;
RT "Crystal structure of Mycobacterium tuberculosis HisB in complex with a
RT ligand.";
RL Submitted (APR-2018) to the PDB data bank.
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 ECO:0000269|PubMed:24311587};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24311587};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:24311587};
CC -!- ACTIVITY REGULATION: Competitive inhibition by 3-amino-1,2,4-triazole
CC (e.g. ATZ). {ECO:0000269|PubMed:24311587}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=122 uM for imidazoleglycerol-phosphate (at pH 7.7 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:24311587};
CC Note=kcat is 1000 sec(-1) with imidazoleglycerol-phosphate as
CC substrate (at pH 7.7 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:24311587};
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, ECO:0000269|PubMed:24311587}.
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; AL123456; CCP44365.1; -; Genomic_DNA.
DR PIR; C70544; C70544.
DR RefSeq; NP_216117.1; NC_000962.3.
DR RefSeq; WP_003407950.1; NZ_NVQJ01000016.1.
DR PDB; 4GQU; X-ray; 2.02 A; A=2-210.
DR PDB; 5XDS; X-ray; 1.75 A; A=2-210.
DR PDB; 5ZQN; X-ray; 1.80 A; A=1-210.
DR PDB; 6KHH; X-ray; 1.65 A; A=10-200.
DR PDB; 6YJH; X-ray; 1.61 A; A=10-200.
DR PDB; 7DDV; X-ray; 2.20 A; A=2-210.
DR PDB; 7DNQ; X-ray; 2.28 A; A=2-210.
DR PDBsum; 4GQU; -.
DR PDBsum; 5XDS; -.
DR PDBsum; 5ZQN; -.
DR PDBsum; 6KHH; -.
DR PDBsum; 6YJH; -.
DR PDBsum; 7DDV; -.
DR PDBsum; 7DNQ; -.
DR AlphaFoldDB; P9WML9; -.
DR SMR; P9WML9; -.
DR STRING; 83332.Rv1601; -.
DR PaxDb; P9WML9; -.
DR DNASU; 886274; -.
DR GeneID; 886274; -.
DR KEGG; mtu:Rv1601; -.
DR TubercuList; Rv1601; -.
DR eggNOG; COG0131; Bacteria.
DR OMA; ARHGLFD; -.
DR PhylomeDB; P9WML9; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Lyase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..210
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_0000158146"
FT CHAIN 9..210
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /evidence="ECO:0000250|UniProtKB:Q02134"
FT /id="PRO_0000445482"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 47..55
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:5ZQN"
FT BINDING 47
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:4GQU"
FT BINDING 73..77
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:5XDS"
FT BINDING 73
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:4GQU"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:4GQU"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:4GQU"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:4GQU"
FT BINDING 176..184
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:5ZQN"
FT BINDING 176
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:4GQU"
FT BINDING 177
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:4GQU"
FT BINDING 180
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24311587,
FT ECO:0007744|PDB:4GQU"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:6YJH"
FT STRAND 20..31
FT /evidence="ECO:0007829|PDB:6YJH"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6YJH"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:6YJH"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:6YJH"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6YJH"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:6YJH"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:6YJH"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:6YJH"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6YJH"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:6YJH"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6YJH"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:6YJH"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:6YJH"
FT HELIX 175..194
FT /evidence="ECO:0007829|PDB:6YJH"
SQ SEQUENCE 210 AA; 22770 MW; E004847AFF01AA89 CRC64;
MTTTQTAKAS RRARIERRTR ESDIVIELDL DGTGQVAVDT GVPFYDHMLT ALGSHASFDL
TVRATGDVEI EAHHTIEDTA IALGTALGQA LGDKRGIRRF GDAFIPMDET LAHAAVDLSG
RPYCVHTGEP DHLQHTTIAG SSVPYHTVIN RHVFESLAAN ARIALHVRVL YGRDPHHITE
AQYKAVARAL RQAVEPDPRV SGVPSTKGAL
