HIS5_VIBCH
ID HIS5_VIBCH Reviewed; 203 AA.
AC Q9KSX0;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase glutaminase subunit;
DE EC=3.5.1.2;
DE AltName: Full=IGP synthase subunit HisH;
DE AltName: Full=ImGP synthase subunit HisH;
DE Short=IGPS subunit HisH;
GN Name=hisH; OrderedLocusNames=VC_1136;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of
CC glutamine to glutamate and ammonia as part of the synthesis of IGP and
CC AICAR. The resulting ammonia molecule is channeled to the active site
CC of HisF (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-
CC phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-
CC amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-
CC erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate;
CC Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475,
CC ChEBI:CHEBI:58525; EC=4.3.2.10;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AE003852; AAF94295.1; -; Genomic_DNA.
DR PIR; C82238; C82238.
DR RefSeq; NP_230781.1; NC_002505.1.
DR RefSeq; WP_000193249.1; NZ_LT906614.1.
DR PDB; 4GUD; X-ray; 1.91 A; A/B=1-203.
DR PDBsum; 4GUD; -.
DR AlphaFoldDB; Q9KSX0; -.
DR SMR; Q9KSX0; -.
DR STRING; 243277.VC_1136; -.
DR MEROPS; C26.965; -.
DR DNASU; 2614406; -.
DR EnsemblBacteria; AAF94295; AAF94295; VC_1136.
DR GeneID; 57739812; -.
DR GeneID; 66939046; -.
DR KEGG; vch:VC_1136; -.
DR PATRIC; fig|243277.26.peg.1085; -.
DR eggNOG; COG0118; Bacteria.
DR HOGENOM; CLU_071837_0_0_6; -.
DR OMA; WVYFVHS; -.
DR BioCyc; VCHO:VC1136-MON; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01748; GATase1_IGP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00278; HisH; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR010139; Imidazole-glycPsynth_HisH.
DR PANTHER; PTHR42701; PTHR42701; 1.
DR Pfam; PF00117; GATase; 1.
DR PIRSF; PIRSF000495; Amidotransf_hisH; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW Glutamine amidotransferase; Histidine biosynthesis; Hydrolase; Lyase;
KW Reference proteome.
FT CHAIN 1..203
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152441"
FT DOMAIN 4..203
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
FT ACT_SITE 187
FT /evidence="ECO:0000250"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4GUD"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4GUD"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4GUD"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:4GUD"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:4GUD"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4GUD"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 160..176
FT /evidence="ECO:0007829|PDB:4GUD"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4GUD"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4GUD"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:4GUD"
SQ SEQUENCE 203 AA; 22274 MW; 2FE3C1D485995700 CRC64;
MTQNVVIIDT GCANISSVKF AIERLGYAVT ISRDPQVVLA ADKLFLPGVG TASEAMKNLT
ERDLIELVKR VEKPLLGICL GMQLLGKLSE EKGQKADEIV QCLGLVDGEV RLLQTGDLPL
PHMGWNTVQV KEGHPLFNGI EPDAYFYFVH SFAMPVGDYT IAQCEYGQPF SAAIQAGNYY
GVQFHPERSS KAGARLIQNF LEL
