xdhB

UniProt ID: Q88F20
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

XdhB is the molybdopterin-cofactor catalytic subunit of the two-subunit XdhAB xanthine dehydrogenase. It houses the purine-base oxidation center and works with the FAD/[2Fe-2S] electron-transfer subunit XdhA to convert hypoxanthine to xanthine and xanthine to urate. These reactions have not been measured directly for the KT2440 complex and are inferred from subunit-specific domain architecture and homologous bacterial XDH biochemistry.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004854 xanthine dehydrogenase activity
IEA
GO_REF:0000003
MODIFY
Summary: XdhB contains the molybdenum catalytic center but requires XdhA to form the complete xanthine dehydrogenase.
Reason: Replace the EC-derived enables relation with contributes_to because XdhB supplies only the molybdopterin catalytic module of the assembled XdhAB electron-transfer system.
Proposed replacements: xanthine dehydrogenase activity
Supporting Evidence:
file:PSEPK/xdhB/xdhB-uniprot.txt
DR InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su.
PMID:11341925
XDH from P. putida 86 consists of 91.0 kDa and 46.2 kDa
file:PSEPK/xdhB/xdhB-deep-research-openscientist.md
encodes the **large molybdenum-cofactor (molybdopterin)-binding catalytic subunit of a two-subunit bacterial xanthine dehydrogenase**
GO:0005506 iron ion binding
IEA
GO_REF:0000002
REMOVE
Summary: The XdhB sequence is assigned to the molybdopterin-binding catalytic subunit rather than the Fe-S-bearing subunit.
Reason: XdhB contains the xanthine-dehydrogenase molybdopterin-binding architecture; the complementary XdhA subunit carries the ferredoxin-type [2Fe-2S] domains. The broad InterPro iron mapping appears to have crossed the multi-subunit enzyme boundary.
Supporting Evidence:
file:PSEPK/xdhB/xdhB-uniprot.txt
DR InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su.
file:PSEPK/xdhA/xdhA-uniprot.txt
DR InterPro; IPR006058; 2Fe2S_fd_BS.
file:PSEPK/xdhB/xdhB-deep-research-openscientist.md
with no FAD- or iron-sulfur-binding regions
GO:0016491 oxidoreductase activity
IEA
GO_REF:0000120
ACCEPT
Summary: XdhB houses the molybdenum center at which substrate oxidation occurs.
Reason: This broad intrinsic redox function is appropriate for the catalytic subunit, while the substrate-specific complete activities are represented separately with contributes_to relations.
Supporting Evidence:
file:PSEPK/xdhB/xdhB-uniprot.txt
DR InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su.
GO:0030151 molybdenum ion binding
IEA
GO_REF:0000002
MODIFY
Summary: XdhB binds molybdenum as part of an organic molybdopterin cofactor rather than as a free ion.
Reason: GO:0043546 describes the biologically relevant cofactor-binding state more accurately.
Proposed replacements: molybdopterin cofactor binding
Supporting Evidence:
file:PSEPK/xdhB/xdhB-uniprot.txt
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
GO:0043546 molybdopterin cofactor binding
ISS NEW
Summary: XdhB is the molybdopterin-binding subunit of bacterial XDH.
Reason: The subunit-specific InterPro architecture supports the cofactor-level replacement for free molybdenum binding.
Supporting Evidence:
file:PSEPK/xdhB/xdhB-uniprot.txt
DR InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su.
GO:0070674 hypoxanthine dehydrogenase activity
ISS NEW
Summary: XdhB contributes the molybdenum catalytic subunit to XdhAB oxidation of hypoxanthine to xanthine.
Reason: The characterized P. putida strain-86 homolog oxidizes hypoxanthine, while the exact KT2440 sequence identifies the corresponding XdhB subunit architecture.
Supporting Evidence:
PMID:11341925
oxidation of hypoxanthine, xanthine, purine, and some aromatic aldehydes, using
file:PSEPK/xdhB/xdhB-uniprot.txt
SubName: Full=Xanthine dehydrogenase subunit XdhB
GO:0009114 hypoxanthine catabolic process
ISS NEW
Summary: XdhB contributes the catalytic center for the XdhAB hypoxanthine-to-xanthine step.
Reason: This is the immediate process for the first purine-base reaction of the homologous two-subunit enzyme.
Supporting Evidence:
PMID:11341925
oxidation of hypoxanthine, xanthine, purine, and some aromatic aldehydes, using
GO:0009115 xanthine catabolic process
ISS NEW
Summary: XdhB contributes the catalytic center for XdhAB oxidation of xanthine to urate.
Reason: Xanthine oxidation is the defining reaction of the homologous P. putida strain-86 XDH.
Supporting Evidence:
PMID:11341925
oxidation of hypoxanthine, xanthine, purine, and some aromatic aldehydes, using
GO:0034418 urate biosynthetic process
ISS NEW
Summary: The XdhAB xanthine oxidation step directly produces urate.
Reason: This process annotation follows from the inferred xanthine dehydrogenase reaction of the assembled KT2440 complex.
Supporting Evidence:
PMID:11341925
oxidation of hypoxanthine, xanthine, purine, and some aromatic aldehydes, using

Core Functions

Molybdopterin-bearing catalytic subunit contributing to XdhAB oxidation of hypoxanthine to xanthine.

Molecular Function:
oxidoreductase activity
Directly Involved In:
Supporting Evidence:
  • file:PSEPK/xdhB/xdhB-uniprot.txt
    DR InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su.
  • PMID:11341925
    oxidation of hypoxanthine, xanthine, purine, and some aromatic aldehydes, using
  • file:PSEPK/xdhB/xdhB-deep-research-openscientist.md
    No direct enzymology on Q88F20 itself.

Molybdopterin-bearing catalytic subunit contributing to XdhAB oxidation of xanthine to urate.

Supporting Evidence:
  • file:PSEPK/xdhB/xdhB-uniprot.txt
    DR InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su.
  • PMID:11341925
    oxidation of hypoxanthine, xanthine, purine, and some aromatic aldehydes, using
  • file:PSEPK/xdhB/xdhB-deep-research-openscientist.md
    No direct enzymology on Q88F20 itself.

References

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Suggested Questions for Experts

Q: Does Q88F20 bind mature molybdopterin cofactor and support both XdhAB purine-base reactions in KT2440?

Suggested experts: bacterial molybdenum-enzyme experts

Suggested Experiments

Experiment: Reconstitute mature KT2440 XdhAB, verify molybdenum-cofactor incorporation into XdhB, and assay hypoxanthine- and xanthine-dependent NAD+ reduction.

Type: enzyme reconstitution assay

Deep Research

OpenScientist

(xdhB-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(xdhB-notes.md)

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