ID A0A1G1JXL8_9BACT Unreviewed; 131 AA.
AC A0A1G1JXL8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=phosphoribosyl-AMP cyclohydrolase {ECO:0000256|ARBA:ARBA00012721};
DE EC=3.5.4.19 {ECO:0000256|ARBA:ARBA00012721};
GN ORFNames=A2987_00525 {ECO:0000313|EMBL:OGW85394.1};
OS Omnitrophica bacterium RIFCSPLOWO2_01_FULL_45_10.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801826 {ECO:0000313|EMBL:OGW85394.1, ECO:0000313|Proteomes:UP000176340};
RN [1] {ECO:0000313|EMBL:OGW85394.1, ECO:0000313|Proteomes:UP000176340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGW85394.1}.
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DR EMBL; MHFL01000007; OGW85394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1JXL8; -.
DR STRING; 1801826.A2987_00525; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000176340; Unassembled WGS sequence.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 1.
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 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OGW85394.1}.
FT DOMAIN 31..103
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
SQ SEQUENCE 131 AA; 15184 MW; 3E16B14126E07964 CRC64;
MIEIFENIKF GKNGLIPAVI QDEKSKKALT LCYMNKKALE KTLKTGKVYV YRRSKGRVMM
KGETSGCVQR VRSVCIDCEG NSLLVKVEQE RAACHEGYFS CYFRKMDKKG RLKTIEKRIF
DPKKVYRVLS E
//
