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Database: UniProt
Entry: A0A3N6WPB1_9ACTN
LinkDB: A0A3N6WPB1_9ACTN
Original site: A0A3N6WPB1_9ACTN 
ID   A0A3N6WPB1_9ACTN        Unreviewed;       219 AA.
AC   A0A3N6WPB1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=EHW97_03805 {ECO:0000313|EMBL:RQN09376.1};
OS   Aeromicrobium camelliae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1538144 {ECO:0000313|EMBL:RQN09376.1, ECO:0000313|Proteomes:UP000275225};
RN   [1] {ECO:0000313|EMBL:RQN09376.1, ECO:0000313|Proteomes:UP000275225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YS17T {ECO:0000313|EMBL:RQN09376.1,
RC   ECO:0000313|Proteomes:UP000275225};
RA   Li F.;
RL   Submitted (NOV-2018) 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:RQN09376.1}.
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DR   EMBL; RQJX01000003; RQN09376.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N6WPB1; -.
DR   OrthoDB; 15077at2; -.
DR   Proteomes; UP000275225; 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   CDD; cd00488; PCD_DCoH; 1.
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   PANTHER; PTHR35908:SF1; CONSERVED PROTEIN; 1.
DR   PANTHER; PTHR35908; HYPOTHETICAL FUSION PROTEIN; 1.
DR   Pfam; PF18029; Glyoxalase_6; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   SUPFAM; SSF55248; PCD-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275225}.
FT   DOMAIN          110..213
FT                   /note="Glyoxalase-like"
FT                   /evidence="ECO:0000259|Pfam:PF18029"
SQ   SEQUENCE   219 AA;  24364 MW;  349714EA367BF9BB CRC64;
     MDGAALDPAV VEEQVDGRHW RVVDRVLHAR FATDGFTTGS RLVEAVGEAA DAARHHPDID
     LRARTVHVRL VSRDVGRLTE RDVALADEIT RIADDLGLET DGVVPQWITI GIDAMDANRL
     RPFWKAVLAY EDDPDDENDL VDPARSGPTV WFQQMDEPRP QRNRIHLDVY VPVDHAERRV
     AAALQAGGTL VTDRYAPSWW VLADAEGNEV CVCTSQISE
//
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