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Database: UniProt
Entry: A0A402A128_9CHLR
LinkDB: A0A402A128_9CHLR
Original site: A0A402A128_9CHLR 
ID   A0A402A128_9CHLR        Unreviewed;       327 AA.
AC   A0A402A128;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JUN-2023, entry version 10.
DE   RecName: Full=phosphoribosyl-AMP cyclohydrolase {ECO:0000256|ARBA:ARBA00012721};
DE            EC=3.5.4.19 {ECO:0000256|ARBA:ARBA00012721};
GN   ORFNames=KTT_25800 {ECO:0000313|EMBL:GCE12721.1};
OS   Tengunoibacter tsumagoiensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Tengunoibacter.
OX   NCBI_TaxID=2014871 {ECO:0000313|EMBL:GCE12721.1, ECO:0000313|Proteomes:UP000287352};
RN   [1] {ECO:0000313|Proteomes:UP000287352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uno3 {ECO:0000313|Proteomes:UP000287352};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:GCE12721.1}.
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DR   EMBL; BIFR01000001; GCE12721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402A128; -.
DR   OrthoDB; 9795769at2; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000287352; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287352}.
FT   DOMAIN          24..98
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF01502"
SQ   SEQUENCE   327 AA;  36686 MW;  202CBE79AD83960C CRC64;
     MLNFDPQGLI PAVVVDDASG AVLMVAFMNE EAVRLTRESG QTHFFSRSRQ KIWHKGEQSG
     NFQEVRAIFV NCEESSLLVR VKQHGDAACH DGYQSCYYRQ LLPDDSYQQI GERVFDPAEV
     YTQLQAHPVE EKEHESPAQI MAEKVAKVRA DVKTQLEDQL RQLYGVYVYL RDNDLSTESN
     TSRLLHESNK EDHSYLASRL ADELQELSDV QTGEHVHSGR ESDTILEGSQ VGYWLFLLAS
     ASTIPYDTFA PHSALLEGYE GGYSEARVIE LRQECLTSFA SQDQEQIIKG LRTGFSLIGW
     ACAQAGVSPE GPAEFDLAQM SRKGLVK
//
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