HIS5_THEMA
ID HIS5_THEMA Reviewed; 201 AA.
AC Q9X0C8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
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;
DE AltName: Full=TmHisH;
GN Name=hisH; OrderedLocusNames=TM_1038;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11264293; DOI=10.1074/jbc.m102012200;
RA Beismann-Driemeyer S., Sterner R.;
RT "Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary
RT structure, steady-state kinetics, and reaction mechanism of the bienzyme
RT complex.";
RL J. Biol. Chem. 276:20387-20396(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=12360532; DOI=10.1002/prot.10161;
RA Korolev S., Skarina T., Evdokimova E., Beasley S., Edwards A.,
RA Joachimiak A., Savchenko A.;
RT "Crystal structure of glutamine amidotransferase from Thermotoga
RT maritima.";
RL Proteins 49:420-422(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=11839304; DOI=10.1016/s0969-2126(02)00702-5;
RA Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M.C.,
RA Sterner R., Wilmanns M.;
RT "Structural evidence for ammonia tunneling across the (beta alpha)(8)
RT barrel of the imidazole glycerol phosphate synthase bienzyme complex.";
RL Structure 10:185-193(2002).
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.
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 -!- ACTIVITY REGULATION: Activated by the binding of either IGP or PRFAR to
CC the active site of HisF.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for glutamine {ECO:0000269|PubMed:11264293};
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.
CC -!- INTERACTION:
CC Q9X0C8; Q9X0C6: hisF; NbExp=2; IntAct=EBI-9026913, EBI-9026911;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; AE000512; AAD36115.1; -; Genomic_DNA.
DR PIR; E72304; E72304.
DR RefSeq; NP_228844.1; NC_000853.1.
DR RefSeq; WP_004080484.1; NZ_CP011107.1.
DR PDB; 1GPW; X-ray; 2.40 A; B/D/F=1-201.
DR PDB; 1K9V; X-ray; 2.40 A; F=1-201.
DR PDB; 1KXJ; X-ray; 2.80 A; A/B=1-201.
DR PDB; 2WJZ; X-ray; 2.60 A; B/D/F=1-201.
DR PDB; 3ZR4; X-ray; 2.41 A; B/D/F=1-201.
DR PDB; 6RTZ; X-ray; 2.87 A; B=1-201.
DR PDB; 6RU0; X-ray; 2.65 A; B/D/F=1-201.
DR PDB; 6YMU; X-ray; 2.11 A; B/D/F=1-201.
DR PDB; 7AC8; X-ray; 2.06 A; B/D/F=1-201.
DR PDBsum; 1GPW; -.
DR PDBsum; 1K9V; -.
DR PDBsum; 1KXJ; -.
DR PDBsum; 2WJZ; -.
DR PDBsum; 3ZR4; -.
DR PDBsum; 6RTZ; -.
DR PDBsum; 6RU0; -.
DR PDBsum; 6YMU; -.
DR PDBsum; 7AC8; -.
DR AlphaFoldDB; Q9X0C8; -.
DR SMR; Q9X0C8; -.
DR DIP; DIP-59019N; -.
DR IntAct; Q9X0C8; 1.
DR STRING; 243274.THEMA_09170; -.
DR MEROPS; C26.965; -.
DR EnsemblBacteria; AAD36115; AAD36115; TM_1038.
DR KEGG; tma:TM1038; -.
DR eggNOG; COG0118; Bacteria.
DR InParanoid; Q9X0C8; -.
DR OMA; WVYFVHS; -.
DR OrthoDB; 1726024at2; -.
DR BioCyc; MetaCyc:MON-468; -.
DR BRENDA; 4.3.1.B2; 6331.
DR BRENDA; 4.3.2.10; 6331.
DR SABIO-RK; Q9X0C8; -.
DR UniPathway; UPA00031; UER00010.
DR EvolutionaryTrace; Q9X0C8; -.
DR Proteomes; UP000008183; Chromosome.
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 Direct protein sequencing; Glutamine amidotransferase;
KW Histidine biosynthesis; Hydrolase; Lyase; Reference proteome.
FT CHAIN 1..201
FT /note="Imidazole glycerol phosphate synthase subunit HisH"
FT /id="PRO_0000152437"
FT DOMAIN 2..201
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 84
FT /note="Nucleophile"
FT ACT_SITE 178
FT ACT_SITE 180
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6YMU"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:7AC8"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:7AC8"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:7AC8"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:7AC8"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:1GPW"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1GPW"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 119..132
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 135..146
FT /evidence="ECO:0007829|PDB:7AC8"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:7AC8"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:7AC8"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:7AC8"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:7AC8"
SQ SEQUENCE 201 AA; 23097 MW; 10957D075094F778 CRC64;
MRIGIISVGP GNIMNLYRGV KRASENFEDV SIELVESPRN DLYDLLFIPG VGHFGEGMRR
LRENDLIDFV RKHVEDERYV VGVCLGMQLL FEESEEAPGV KGLSLIEGNV VKLRSRRLPH
MGWNEVIFKD TFPNGYYYFV HTYRAVCEEE HVLGTTEYDG EIFPSAVRKG RILGFQFHPE
KSSKIGRKLL EKVIECSLSR R
