ID E6VZY3_PSEA9 Unreviewed; 124 AA.
AC E6VZY3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=Daes_3073 {ECO:0000313|EMBL:ADU64065.1};
OS Pseudodesulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2)
OS (Desulfovibrio aespoeensis).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU64065.1, ECO:0000313|Proteomes:UP000002191};
RN [1] {ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pedersen K., Jagevall S.,
RA Hazen T., Woyke T.;
RT "Complete sequence of Desulfovibrio aespoeensis Aspo-2.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU64065.1, ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RX PubMed=24874683;
RA Pedersen K., Bengtsson A., Edlund J., Rabe L., Hazen T., Chakraborty R.,
RA Goodwin L., Shapiro N.;
RT "Complete Genome Sequence of the Subsurface, Mesophilic Sulfate-Reducing
RT Bacterium Desulfovibrio aespoeensis Aspo-2.";
RL Genome Announc. 2:e00509-14(2014).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-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;
CC Evidence={ECO:0000256|HAMAP-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 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}.
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DR EMBL; CP002431; ADU64065.1; -; Genomic_DNA.
DR RefSeq; WP_013515966.1; NC_014844.1.
DR AlphaFoldDB; E6VZY3; -.
DR STRING; 643562.Daes_3073; -.
DR KEGG; das:Daes_3073; -.
DR eggNOG; COG0139; Bacteria.
DR HOGENOM; CLU_048577_5_3_7; -.
DR OrthoDB; 9795769at2; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000002191; 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; 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 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 Zinc {ECO:0000256|HAMAP-Rule:MF_01021}.
FT DOMAIN 27..101
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 75
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 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 92
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 99
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 124 AA; 14208 MW; 05964E2701CBE334 CRC64;
MIRPDFEKMD GLVPAIAQDA ETGEVLMMAY MNEEAWNKTL ESGEVHYWSR SRQELWHKGG
TSGHTQTVKS IRIDCDDDTV LFLIDQIGGA ACHKGYRSCF YRELKDGEVR ECSPLVFDPK
EVYK
//
