ID HIS3_ALCBS Reviewed; 142 AA. AC Q0VML6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 28-JAN-2026, entry version 103. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01021}; DE Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01021}; DE EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01021}; GN Name=hisI {ECO:0000255|HAMAP-Rule:MF_01021}; GN OrderedLocusNames=ABO_2134; OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / OS SK2). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Oceanospirillales; Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2; RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O., RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., RA Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium RT Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of CC phosphoribosyl-AMP. {ECO:0000255|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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01021}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01021}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01021}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01021}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01021}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000255|HAMAP- CC Rule:MF_01021}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM286690; CAL17582.1; -; Genomic_DNA. DR RefSeq; WP_011589412.1; NC_008260.1. DR AlphaFoldDB; Q0VML6; -. DR SMR; Q0VML6; -. DR STRING; 393595.ABO_2134; -. DR KEGG; abo:ABO_2134; -. DR eggNOG; COG0139; Bacteria. DR HOGENOM; CLU_048577_5_0_6; -. DR OrthoDB; 9795769at2; -. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000008871; 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-ARBA. 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; 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; PRK00051.1; 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; Cytoplasm; Histidine biosynthesis; Hydrolase; KW Magnesium; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..142 FT /note="Phosphoribosyl-AMP cyclohydrolase" FT /id="PRO_0000319680" FT BINDING 92 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 93 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 94 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 96 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" SQ SEQUENCE 142 AA; 15938 MW; 1AB3214F6B1C4E9F CRC64; MFKHNEQQPE GFQISLKEAL DNLAFNDAGL VAAIAQQHDS GEVLMMAWMN REAIEETLAT GRVCYFSRSR GKLWRKGESS GQVQTLKELR IDCDGDALLV KVDQTGSACH TGRRDCFYWK ADANNVTIDK APIKDPKELY GK //