ID   A0A0Q9KS74_9MICO        Unreviewed;       235 AA.
AC   A0A0Q9KS74;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Putative pterin-4-alpha-carbinolamine dehydratase {ECO:0000256|ARBA:ARBA00021735};
DE            EC=4.2.1.96 {ECO:0000256|ARBA:ARBA00013252};
GN   ORFNames=ASG74_09985 {ECO:0000313|EMBL:KRE42696.1};
OS   Knoellia sp. Soil729.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE42696.1, ECO:0000313|Proteomes:UP000051965};
RN   [1] {ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE42696.1, ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|EMBL:KRE42696.1,
RC   ECO:0000313|Proteomes:UP000051965};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin =
CC         (6R)-L-erythro-6,7-dihydrobiopterin + H2O; Xref=Rhea:RHEA:11920,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15642, ChEBI:CHEBI:43120; EC=4.2.1.96;
CC         Evidence={ECO:0000256|ARBA:ARBA00001554};
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000256|ARBA:ARBA00006472}.
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:KRE42696.1}.
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DR   EMBL; LMSA01000002; KRE42696.1; -; Genomic_DNA.
DR   RefSeq; WP_056142201.1; NZ_LMSA01000002.1.
DR   AlphaFoldDB; A0A0Q9KS74; -.
DR   STRING; 1736394.ASG74_09985; -.
DR   OrthoDB; 15077at2; -.
DR   Proteomes; UP000051965; Unassembled WGS sequence.
DR   GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR   Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR041581; Glyoxalase_6.
DR   InterPro; IPR036428; PCD_sf.
DR   InterPro; IPR001533; Pterin_deHydtase.
DR   Pfam; PF18029; Glyoxalase_6; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF55248; PCD-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          120..222
FT                   /note="Glyoxalase-like"
FT                   /evidence="ECO:0000259|Pfam:PF18029"
SQ   SEQUENCE   235 AA;  25032 MW;  54EC435BD7FA6AC0 CRC64;
     MDMLRGEQIA AADLAEWRKL AQGLHARYLV DDFGAGARFV AAVGEAGDEL EHHPRVFMGP
     RHVDLKLITD DAIYRDDEGT EYVVEWPTQQ DVDLARRITE IAGEQGLTAD PASVSMVELG
     LDTGDSATIA PVWAALLTGN AEAQGHGSPG DEVRDATGRV PNLWFGDSPG EDATRQRFHV
     EVYVAPEVLE QRVAAAVAAG GTVVDDSDAP SLTVIADQDG NRGVICADMS AARKG
//