ID A0A091KLD1_9GRUI Unreviewed; 102 AA.
AC A0A091KLD1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pterin-4-alpha-carbinolamine dehydratase {ECO:0000256|ARBA:ARBA00040209};
DE EC=4.2.1.96 {ECO:0000256|ARBA:ARBA00013252};
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase {ECO:0000256|ARBA:ARBA00030497};
DE AltName: Full=Dimerization cofactor of hepatocyte nuclear factor 1-alpha {ECO:0000256|ARBA:ARBA00042969};
DE AltName: Full=Phenylalanine hydroxylase-stimulating protein {ECO:0000256|ARBA:ARBA00042558};
DE AltName: Full=Pterin carbinolamine dehydratase {ECO:0000256|ARBA:ARBA00031023};
DE Flags: Fragment;
GN ORFNames=N324_12902 {ECO:0000313|EMBL:KFP40323.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP40323.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP40323.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP40323.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000256|ARBA:ARBA00006472}.
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DR EMBL; KK746292; KFP40323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KLD1; -.
DR Proteomes; UP000053330; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00914; PCD_DCoH_subfamily_b; 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; PTHR12599; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR PANTHER; PTHR12599:SF13; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; PCD-like; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053330};
KW Tetrahydrobiopterin biosynthesis {ECO:0000256|ARBA:ARBA00023007};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP40323.1"
FT NON_TER 102
FT /evidence="ECO:0000313|EMBL:KFP40323.1"
SQ SEQUENCE 102 AA; 11708 MW; 25E6ED62D0697562 CRC64;
AGKAHRLSAE EREQLLPNLR AVGWNEVEGR DAIFKEFHFK DFNRAFGFMT RVALQAEKLD
HHPEWFNVYN KVHITLSTHE CGGLSERDIN LASFIEQVAA SL
//
