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Database: UniProt
Entry: A0A1V2QN57_9PSEU
LinkDB: A0A1V2QN57_9PSEU
Original site: A0A1V2QN57_9PSEU 
ID   A0A1V2QN57_9PSEU        Unreviewed;       220 AA.
AC   A0A1V2QN57;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=ALI22I_14300 {ECO:0000313|EMBL:ONI89671.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI89671.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI89671.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI89671.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI89671.1}.
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DR   EMBL; MTQP01000055; ONI89671.1; -; Genomic_DNA.
DR   RefSeq; WP_077005992.1; NZ_MTQP01000055.1.
DR   AlphaFoldDB; A0A1V2QN57; -.
DR   STRING; 1933778.ALI22I_14300; -.
DR   OrthoDB; 15077at2; -.
DR   Proteomes; UP000188617; 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   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; SSF55248; PCD-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188617}.
FT   DOMAIN          110..213
FT                   /note="Glyoxalase-like"
FT                   /evidence="ECO:0000259|Pfam:PF18029"
SQ   SEQUENCE   220 AA;  23989 MW;  7C6C6A829E20EF68 CRC64;
     MTERISPRQF HEADGVEDWR VLGEGACAYF RTGSFAAGAR LVAAIGESAG VDDHQPDVDV
     RREGVYVRLI TTADDYWGLT ERDLQSARRI SAVARGLGVA ADPSAVQTVQ ISIDALVAPE
     VMPFWRAVLG YVDRGDSPED LVDPLGRGAN LWFQRMDAPR PQRNRIHVDV WVPHDRAEAR
     IAAALAAGGR LVSDAHAPGW WTLADAEGNE VDVATWVDHG
//
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