HIS3_METTH
ID HIS3_METTH Reviewed; 138 AA.
AC O26347;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01021};
DE Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01021};
DE EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01021};
GN Name=hisI {ECO:0000255|HAMAP-Rule:MF_01021}; OrderedLocusNames=MTH_245;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH CADMIUM, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP METAL-BINDING SITES.
RX PubMed=16042384; DOI=10.1021/bi050472w;
RA Sivaraman J., Myers R.S., Boju L., Sulea T., Cygler M., Jo Davisson V.,
RA Schrag J.D.;
RT "Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-
RT AMP cyclohydrolase HisI.";
RL Biochemistry 44:10071-10080(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021,
CC ECO:0000269|PubMed:16042384}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01021, ECO:0000269|PubMed:16042384};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:16042384};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305|PubMed:16042384};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:16042384};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:16042384};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for phosphoribosyl-AMP {ECO:0000269|PubMed:16042384};
CC Note=kcat is 8 sec(-1).;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000255|HAMAP-Rule:MF_01021}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01021,
CC ECO:0000269|PubMed:16042384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01021}.
CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000255|HAMAP-
CC Rule:MF_01021}.
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DR EMBL; AE000666; AAB84751.1; -; Genomic_DNA.
DR PIR; F69130; F69130.
DR PDB; 1ZPS; X-ray; 1.70 A; A/B=1-138.
DR PDBsum; 1ZPS; -.
DR AlphaFoldDB; O26347; -.
DR SMR; O26347; -.
DR STRING; 187420.MTH_245; -.
DR EnsemblBacteria; AAB84751; AAB84751; MTH_245.
DR KEGG; mth:MTH_245; -.
DR PATRIC; fig|187420.15.peg.214; -.
DR HOGENOM; CLU_048577_5_1_2; -.
DR OMA; TGYRSCF; -.
DR UniPathway; UPA00031; UER00008.
DR EvolutionaryTrace; O26347; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.20.810; -; 1.
DR HAMAP; MF_01021; HisI; 1.
DR InterPro; IPR026660; PRA-CH.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR Pfam; PF01502; PRA-CH; 1.
DR SUPFAM; SSF141734; SSF141734; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..138
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /id="PRO_0000136511"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:1ZPS"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:1ZPS"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1ZPS"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1ZPS"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1ZPS"
FT TURN 69..73
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 88..99
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1ZPS"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1ZPS"
SQ SEQUENCE 138 AA; 15458 MW; ABE62FDD2235C067 CRC64;
MIKSKGDVNI LLNFRHNING EDLIIAVAQD HETGEVLMVA YMNREALRRT LETGTAHYWS
TSRGKLWLKG ESSGHVQRVK DVLVDCDGDA VVLKVEQEGG ACHTGYRSCF YRSIDGDELK
VREDAVKVFD PEEIYGDG
