ID A0A2K9LFU1_9GAMM Unreviewed; 144 AA.
AC A0A2K9LFU1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=Kalk_01255 {ECO:0000313|EMBL:AUM11142.1};
OS Ketobacter alkanivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=1917421 {ECO:0000313|EMBL:AUM11142.1, ECO:0000313|Proteomes:UP000235116};
RN [1] {ECO:0000313|Proteomes:UP000235116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GI5 {ECO:0000313|Proteomes:UP000235116};
RA Kim S.-J., Rhee S.-K.;
RT "Direct submision.";
RL Submitted (AUG-2017) 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 -!- 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; CP022684; AUM11142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9LFU1; -.
DR KEGG; kak:Kalk_01255; -.
DR OrthoDB; 9795769at2; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000235116; 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; 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 PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 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:UP000235116};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01021}.
FT DOMAIN 47..120
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 95
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 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 98
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 144 AA; 16426 MW; 8BBE05C0F3C037EA CRC64;
MNRFKALEKS EVGFRTPLDE MMRHIKFNDQ GLIPAVAQQF DTKEVLMMAW MNRDALQETL
DTGRVCYWSR SRGGLWRKGE SSGQIQLLKT LALDCDGDTV LMQVDQKGPA CHTGRRSCFF
YQVDGSEITV NADVLISPDE LYKK
//
