ID   F0SNF5_RUBBR            Unreviewed;       153 AA.
AC   F0SNF5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   04-NOV-2026, entry version 70.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021};
DE            Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01021};
DE            EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01021};
GN   Name=hisI {ECO:0000256|HAMAP-Rule:MF_01021};
GN   OrderedLocusNames=Plabr_0159 {ECO:0000313|EMBL:ADY57789.1};
OS   Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM
OS   15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis).
OC   Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
OC   Planctomycetales; Planctomycetaceae; Rubinisphaera.
OX   NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY57789.1, ECO:0000313|Proteomes:UP000006860};
RN   [1] {ECO:0000313|Proteomes:UP000006860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448
RC   {ECO:0000313|Proteomes:UP000006860};
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Planctomyces brasiliensis DSM 5305.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC       phosphoribosyl-AMP. {ECO:0000256|HAMAP-Rule:MF_01021}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000024, ECO:0000256|HAMAP-
CC         Rule:MF_01021};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC         ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001460};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01021};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01021};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01021};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01021};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC       {ECO:0000256|ARBA:ARBA00005204}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000256|ARBA:ARBA00005169, ECO:0000256|HAMAP-Rule:MF_01021}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021}.
CC   -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP-
CC       Rule:MF_01021}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC       {ECO:0000256|ARBA:ARBA00007731}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC       {ECO:0000256|ARBA:ARBA00008299}.
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DR   EMBL; CP002546; ADY57789.1; -; Genomic_DNA.
DR   RefSeq; WP_013626533.1; NC_015174.1.
DR   AlphaFoldDB; F0SNF5; -.
DR   STRING; 756272.Plabr_0159; -.
DR   KEGG; pbs:Plabr_0159; -.
DR   eggNOG; COG0139; Bacteria.
DR   HOGENOM; CLU_048577_5_0_0; -.
DR   OMA; AGACHTG; -.
DR   OrthoDB; 9795769at2; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000006860; 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:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.10.20.810:FF:000001; Histidine biosynthesis bifunctional protein HisIE; 1.
DR   Gene3D; 4.10.80.70; -; 1.
DR   Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 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   NCBIfam; NF000768; hisI; 1.
DR   PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR42945:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 1.
DR   Pfam; PF01502; PRA-CH; 1.
DR   SUPFAM; SSF141734; HisI-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01021};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01021};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01021};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01021};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01021};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006860};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01021}.
FT   DOMAIN          46..120
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF01502"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   BINDING         95
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
SQ   SEQUENCE   153 AA;  17182 MW;  4AA442B3D052DB6B CRC64;
     MSESLQFAAR EDKSQVEQGD QLAPKFDSSG LIPAIATDHA TGELLMVAYM NEEAFKKTIE
     IGEAVYYSRS RQEMWHKGAT SGHTQKVIEL RVDCDQDAVW LRVDQQGSGA CHVGYRSCFY
     RAVDRDNLSS DKPVGLKLAE KEKAYDPSKV YKK
//