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Database: UniProt
Entry: U9VRY4_9CYAN
LinkDB: U9VRY4_9CYAN
Original site: U9VRY4_9CYAN 
ID   U9VRY4_9CYAN            Unreviewed;       127 AA.
AC   U9VRY4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=N836_15390 {ECO:0000313|EMBL:ESA34802.1};
OS   Leptolyngbya sp. Heron Island J.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA34802.1, ECO:0000313|Proteomes:UP000017515};
RN   [1] {ECO:0000313|EMBL:ESA34802.1, ECO:0000313|Proteomes:UP000017515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Heron Island J {ECO:0000313|EMBL:ESA34802.1,
RC   ECO:0000313|Proteomes:UP000017515};
RX   PubMed=24503993;
RA   Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA   Fromme P.;
RT   "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT   Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL   Genome Announc. 2:e01166-e01113(2014).
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}.
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:ESA34802.1}.
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DR   EMBL; AWNH01000071; ESA34802.1; -; Genomic_DNA.
DR   RefSeq; WP_023074420.1; NZ_AWNH01000071.1.
DR   AlphaFoldDB; U9VRY4; -.
DR   STRING; 1385935.N836_15390; -.
DR   PATRIC; fig|1385935.3.peg.4551; -.
DR   eggNOG; COG2154; Bacteria.
DR   OrthoDB; 9794987at2; -.
DR   Proteomes; UP000017515; Unassembled WGS sequence.
DR   GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR   CDD; cd00913; PCD_DCoH_subfamily_a; 1.
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; PTHR42805; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR42805:SF1; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE-RELATED; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017515}.
SQ   SEQUENCE   127 AA;  13926 MW;  C745C5703410A83B CRC64;
     MSNLLTSQIC IPCSGKVPPA SDAEVAELKP QIPDWDIIPV DGVQQLQRVY NFSNFKTALE
     FTNKVGEIAE AEQHHPALLT EWGKVTVTWW THALNGLHRN DFIMAAKTDA AAQGLTSDAP
     APSHLHD
//
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