ID A0A1C5JPG0_9ACTN Unreviewed; 243 AA.
AC A0A1C5JPG0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=GA0070614_5004 {ECO:0000313|EMBL:SCG72475.1};
OS Micromonospora coxensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG72475.1, ECO:0000313|Proteomes:UP000198215};
RN [1] {ECO:0000313|EMBL:SCG72475.1, ECO:0000313|Proteomes:UP000198215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG72475.1,
RC ECO:0000313|Proteomes:UP000198215};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; LT607753; SCG72475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5JPG0; -.
DR OrthoDB; 15077at2; -.
DR Proteomes; UP000198215; Chromosome i.
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}.
FT DOMAIN 117..220
FT /note="Glyoxalase-like"
FT /evidence="ECO:0000259|Pfam:PF18029"
FT REGION 222..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 25877 MW; F6AE930BD3A64C45 CRC64;
MTEGATQVTG RVTPRQFHES AGVRDWRVLG DGVSTYFRTG SFAAGARLVR AIGELAGLDE
HHPDVDVRHA GVTVRLVTIT DDHFGLTGRD VELARRISAV ARDLGLVADP SAVQHVQVTV
DALVGPEVTP FWRALLGYVD RAGSPEDLID PGGRGPSFWF QRMDAPRPQR NRVHVDVWVP
YDRAEERVAA ALAAGGRLVT DAYAPSYWVL ADAEGNEACV GAAGGTGPDP APVDGDTHGQ
AVA
//