hisI

UniProt ID: Q88D15
Organism: Pseudomonas putida KT2440
Review Status: DRAFT
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Gene Description

hisI encodes phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19), which hydrolyzes the adenine ring of phosphoribosyl-AMP in the third reaction of L-histidine biosynthesis. The 130-residue Pseudomonas putida KT2440 enzyme is a standalone cyclohydrolase rather than a HisIE fusion and binds magnesium and zinc ions. The preceding phosphoribosyl-ATP diphosphatase reaction is carried out by the adjacent standalone HisE protein, Q88D14.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000105 L-histidine biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: HisI performs the third reaction of the PRPP-to-histidine pathway.
Reason: The reviewed UniProt entry and UniPathway assignment place the exact cyclohydrolase reaction at step 3 of 9 in L-histidine biosynthesis.
GO:0000287 magnesium ion binding
IEA
GO_REF:0000104
KEEP AS NON CORE
Summary: Magnesium binding is supported for the standalone cyclohydrolase.
Reason: UniRule records one Mg2+ ion per subunit. This is relevant catalytic context but is less informative than the specific cyclohydrolase activity.
GO:0004635 phosphoribosyl-AMP cyclohydrolase activity
IEA
GO_REF:0000120
ACCEPT
Summary: This is the defining HisI activity in KT2440.
Reason: GO:0004635 matches EC 3.5.4.19, RHEA:20049, the reviewed product name, and the HisI/PRA-CH family assignments. The support cited is the curated HAMAP MF_01021 FUNCTION statement and the PRA-CH family/domain classifications (rule-based, not a KT2440 assay).
Supporting Evidence:
file:PSEPK/hisI/hisI-uniprot.txt
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
file:PSEPK/hisI/hisI-uniprot.txt
HAMAP; MF_01021; HisI; 1.
file:PSEPK/hisI/hisI-uniprot.txt
Pfam; PF01502; PRA-CH; 1.
GO:0004636 phosphoribosyl-ATP diphosphatase activity
IEA
GO_REF:0000117
REMOVE
Summary: The diphosphatase activity belongs to the separate HisE protein in KT2440.
Reason: This ARBA assignment appears to have propagated across a family that also contains bifunctional HisIE proteins. Q88D15 is a 130-residue standalone phosphoribosyl-AMP cyclohydrolase, whereas adjacent Q88D14 is the reviewed standalone phosphoribosyl-ATP diphosphatase with EC 3.6.1.31 and RHEA:22828.
Supporting Evidence:
file:PSEPK/hisE/hisE-uniprot.txt
Full=Phosphoribosyl-ATP pyrophosphatase
file:PSEPK/hisI/hisI-deep-research-openscientist.md
*hisI* is a **standalone monofunctional gene** (PP_5014, 130 aa) sitting adjacent to a separate monofunctional *hisE* gene
GO:0005737 cytoplasm
IEA
GO_REF:0000120
KEEP AS NON CORE
Summary: HisI is a soluble cytoplasmic biosynthetic enzyme.
Reason: The location is supported by UniProt but is contextual rather than the core biochemical function.
GO:0008270 zinc ion binding
IEA
GO_REF:0000104
KEEP AS NON CORE
Summary: Zinc binding is supported for the standalone cyclohydrolase.
Reason: UniRule records one Zn2+ ion per subunit. This is supporting cofactor context rather than a pathway-defining activity.

Core Functions

Hydrolyzes the adenine ring of phosphoribosyl-AMP to form the ProFAR intermediate in L-histidine biosynthesis.

Supporting Evidence:
  • file:PSEPK/hisI/hisI-uniprot.txt
    Catalyzes the hydrolysis of the adenine ring of
  • file:PSEPK/hisI/hisI-deep-research-openscientist.md
    catalyzes the third step of the *de novo* L-histidine biosynthetic pathway

References

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Deep Research

OpenScientist

(hisI-deep-research-openscientist.md)

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