HIS7_STAAN
ID HIS7_STAAN Reviewed; 192 AA.
AC P64373; Q99QW5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=SA2468;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP COFACTOR.
RA Kim Y., Quartey P., Holzle D., Collart F., Joachimiak A.;
RT "Crystal structure of imidazoleglycerol-phosphate dehydratase from
RT Staphylococcus aureus subsp. aureus N315.";
RL Submitted (JUL-2005) 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|Ref.2};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305|Ref.2};
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; BA000018; BAB43774.1; -; Genomic_DNA.
DR PIR; D90076; D90076.
DR RefSeq; WP_000640266.1; NC_002745.2.
DR PDB; 2AE8; X-ray; 2.01 A; A/B/C/D/E/F=1-192.
DR PDBsum; 2AE8; -.
DR AlphaFoldDB; P64373; -.
DR SMR; P64373; -.
DR EnsemblBacteria; BAB43774; BAB43774; BAB43774.
DR KEGG; sau:SA2468; -.
DR HOGENOM; CLU_044308_3_0_9; -.
DR OMA; ARHGLFD; -.
DR UniPathway; UPA00031; UER00011.
DR EvolutionaryTrace; P64373; -.
DR Proteomes; UP000000751; 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: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 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.
FT CHAIN 1..192
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_0000158167"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 36..44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 36
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8"
FT BINDING 62..66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 134
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8"
FT BINDING 158..166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 158
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8"
FT BINDING 159
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2AE8"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:2AE8"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2AE8"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:2AE8"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2AE8"
FT HELIX 61..82
FT /evidence="ECO:0007829|PDB:2AE8"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:2AE8"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:2AE8"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2AE8"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2AE8"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:2AE8"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:2AE8"
FT HELIX 157..175
FT /evidence="ECO:0007829|PDB:2AE8"
SQ SEQUENCE 192 AA; 21456 MW; 68F9A068091BA280 CRC64;
MIYQKQRNTA ETQLNISISD DQSPSHINTG VGFLNHMLTL FTFHSGLSLN IEAQGDIDVD
DHHVTEDIGI VIGQLLLEMI KDKKHFVRYG TMYIPMDETL ARVVVDISGR PYLSFNASLS
KEKVGTFDTE LVEEFFRAVV INARLTTHID LIRGGNTHHE IEAIFKAFSR ALGIALTATD
DQRVPSSKGV IE
