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Database: UniProt
Entry: A0A3M2JL72_9CELL
LinkDB: A0A3M2JL72_9CELL
Original site: A0A3M2JL72_9CELL 
ID   A0A3M2JL72_9CELL        Unreviewed;       227 AA.
AC   A0A3M2JL72;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=EBM89_06405 {ECO:0000313|EMBL:RMI12966.1};
OS   Cellulomonas triticagri.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=2483352 {ECO:0000313|EMBL:RMI12966.1, ECO:0000313|Proteomes:UP000269289};
RN   [1] {ECO:0000313|EMBL:RMI12966.1, ECO:0000313|Proteomes:UP000269289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY56 {ECO:0000313|EMBL:RMI12966.1,
RC   ECO:0000313|Proteomes:UP000269289};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of actinobacteria from
RT   wheat.";
RL   Submitted (OCT-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:RMI12966.1}.
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DR   EMBL; RFFI01000025; RMI12966.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2JL72; -.
DR   OrthoDB; 15077at2; -.
DR   Proteomes; UP000269289; 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; 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:UP000269289}.
FT   DOMAIN          113..219
FT                   /note="Glyoxalase-like"
FT                   /evidence="ECO:0000259|Pfam:PF18029"
SQ   SEQUENCE   227 AA;  23963 MW;  8BEAE935F3F5A4A0 CRC64;
     MDTESDGAVG AGDVTRAVDP RHWRVLLRWV QGAFRTPDLA TGAAFAARVA VEAERVGSHP
     DITLRPDLVQ VRATAPDARG IGAADVALAL AVSAVADDMG LPGAPERLTS QEVAIDALDI
     PAVAPFWRAV LGYVPEPGTD PDDPALADPW ALGPGYWFQQ MDAPRPQRNR IHLDVTVPHD
     QAEARVAAAL AAGGTLLSAD RAPAFWVLAD PEGNEACVCT WQARGED
//
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