ID A0A1B3ZGC7_9SPHN Unreviewed; 101 AA.
AC A0A1B3ZGC7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Putative pterin-4-alpha-carbinolamine dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE Short=PHS {ECO:0000256|HAMAP-Rule:MF_00434};
DE EC=4.2.1.96 {ECO:0000256|HAMAP-Rule:MF_00434};
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE AltName: Full=Pterin carbinolamine dehydratase {ECO:0000256|HAMAP-Rule:MF_00434};
DE Short=PCD {ECO:0000256|HAMAP-Rule:MF_00434};
GN ORFNames=AWL63_03540 {ECO:0000313|EMBL:AOH86484.1};
OS Sphingomonas panacis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1560345 {ECO:0000313|EMBL:AOH86484.1, ECO:0000313|Proteomes:UP000094256};
RN [1] {ECO:0000313|EMBL:AOH86484.1, ECO:0000313|Proteomes:UP000094256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY99 {ECO:0000313|EMBL:AOH86484.1,
RC ECO:0000313|Proteomes:UP000094256};
RA Kim Y.J., Yang D.C., Sing P.;
RT "Complete genome and mega plasmid sequence of Sphingomonas panacis DCY99
RT elicits systemic resistance in rice to Xanthomonas oryzae.";
RL Submitted (JAN-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, ECO:0000256|HAMAP-
CC Rule:MF_00434};
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000256|ARBA:ARBA00006472, ECO:0000256|HAMAP-
CC Rule:MF_00434}.
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DR EMBL; CP014168; AOH86484.1; -; Genomic_DNA.
DR RefSeq; WP_069206996.1; NZ_CP014168.1.
DR AlphaFoldDB; A0A1B3ZGC7; -.
DR STRING; 1560345.AWL63_03540; -.
DR KEGG; span:AWL63_03540; -.
DR OrthoDB; 9794987at2; -.
DR Proteomes; UP000094256; Chromosome.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR HAMAP; MF_00434; Pterin_4_alpha; 1.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR001533; Pterin_deHydtase.
DR PANTHER; PTHR12599; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR PANTHER; PTHR12599:SF0; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; PCD-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00434}.
SQ SEQUENCE 101 AA; 11454 MW; F075A1EEE96D9643 CRC64;
MVAALTSNER HDALAKLPAW SFDEAKDALY RYAEFADFAE AFGTMARIAI EAEKVGHHPE
WLNVYNRLQI WLTTHDAGNK VSARDVDLAS TIESFLPEER M
//
