ID   KHS_FUSSH               Reviewed;         350 AA.
AC   Q00870;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Kievitone hydratase;
DE            Short=KHase;
DE            EC=4.2.1.95;
DE   Flags: Precursor;
GN   Name=khs;
OS   Fusarium solani subsp. phaseoli (Nectria haematococca).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=120645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, INDUCTION,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 60860 / FB; TISSUE=Mycelium;
RX   PubMed=7655061; DOI=10.1094/mpmi-8-0388;
RA   Li D., Chung K.R., Smith D.A., Schardl C.L.;
RT   "The Fusarium solani gene encoding kievitone hydratase, a secreted enzyme
RT   that catalyzes detoxification of a bean phytoalexin.";
RL   Mol. Plant Microbe Interact. 8:388-397(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP   FUNCTION, INDUCTION, SUBUNIT, AND GLYCOSYLATION.
RX   PubMed=1366757; DOI=10.1016/0031-9422(90)87088-c;
RA   Turbek C.S., Li D.X., Choi G.H., Schardl C.L., Smith D.A.;
RT   "Induction and purification of kievitone hydratase from Fusarium solani f.
RT   sp. phaseoli.";
RL   Phytochemistry 29:2841-2846(1990).
CC   -!- FUNCTION: Converts fungitoxic kievitone to the less toxic kievitone
CC       hydrate, and thereby protects the pathogenic fungus against this
CC       phytoalexin. {ECO:0000269|PubMed:1366757, ECO:0000269|PubMed:7655061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=kievitone hydrate = H2O + kievitone; Xref=Rhea:RHEA:23604,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16832, ChEBI:CHEBI:17529; EC=4.2.1.95;
CC         Evidence={ECO:0000269|PubMed:1366757, ECO:0000269|PubMed:7655061};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1366757}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1366757,
CC       ECO:0000269|PubMed:7655061}.
CC   -!- INDUCTION: Up-regulated by biochanin and phaseollinisoflavan.
CC       {ECO:0000269|PubMed:1366757, ECO:0000269|PubMed:7655061}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:1366757}.
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DR   EMBL; L39639; AAA87627.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00870; -.
DR   SMR; Q00870; -.
DR   KEGG; ag:AAA87627; -.
DR   BioCyc; MetaCyc:MON-19168; -.
DR   BRENDA; 4.2.1.95; 2361.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050015; F:kievitone hydratase activity; IDA:UniProtKB.
DR   GO; GO:0051410; P:detoxification of nitrogen compound; IDA:UniProtKB.
DR   GO; GO:0052316; P:phytoalexin catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.40.370.10; -; 2.
DR   InterPro; IPR023374; AttH-like_dom_sf.
PE   1: Evidence at protein level;
KW   Detoxification; Direct protein sequencing; Glycoprotein; Lyase; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:1366757"
FT   CHAIN           20..350
FT                   /note="Kievitone hydratase"
FT                   /id="PRO_5000142792"
SQ   SEQUENCE   350 AA;  38970 MW;  CE09B07A7B34C91B CRC64;
     MMISSVLVAG VVAVSAALAS KHPKQYSFKP EDAETIWNGD IPVLYDFGDS QSASYSGSWW
     TSSYITGTNG EQYLVISHYL DTPVFTYFRA STLNLETLDY NQFITLGNNT ANSTTLDVKV
     GDNGIQSLTA DNISQQRAYA NDENVTFDIT FDATSRVISN AGAGVFQFGP SITYEWGLPN
     CRTQGSVTDT GGKNITVDPA KSFTWYDRQW GTAAVTSGNW TWFQMHIPET SYKLSVWIID
     NDVTNQFSRF ATIRGDNDEF QVLPLEWKPI YDRTYQSTAA DILYPLDWEL DISGFGVFQL
     SSILDDQEIV GTTAIQTAYE GFVTFNGTVH NKKVQGYGLV EVVYSNWESL