ID A0A1D3L167_9EURY Unreviewed; 384 AA.
AC A0A1D3L167;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-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=MCBB_0848 {ECO:0000313|EMBL:SCG85412.1};
OS Methanobacterium congolense.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=118062 {ECO:0000313|EMBL:SCG85412.1, ECO:0000313|Proteomes:UP000094707};
RN [1] {ECO:0000313|EMBL:SCG85412.1, ECO:0000313|Proteomes:UP000094707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Buetzberg {ECO:0000313|EMBL:SCG85412.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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; LT607756; SCG85412.1; -; Genomic_DNA.
DR RefSeq; WP_071906578.1; NZ_LT607756.1.
DR AlphaFoldDB; A0A1D3L167; -.
DR STRING; 118062.MCBB_0848; -.
DR GeneID; 30411697; -.
DR KEGG; mcub:MCBB_0848; -.
DR PATRIC; fig|129848.4.peg.850; -.
DR OrthoDB; 10495at2157; -.
DR Proteomes; UP000094707; Chromosome I.
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; cd00488; PCD_DCoH; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR HAMAP; MF_00434; Pterin_4_alpha; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR001533; Pterin_deHydtase.
DR PANTHER; PTHR12697:SF5; DEOXYHYPUSINE HYDROXYLASE; 1.
DR PANTHER; PTHR12697; PBS LYASE HEAT-LIKE PROTEIN; 1.
DR Pfam; PF13646; HEAT_2; 2.
DR Pfam; PF01329; Pterin_4a; 1.
DR SMART; SM00567; EZ_HEAT; 5.
DR SUPFAM; SSF48371; ARM repeat; 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:UP000094707}.
SQ SEQUENCE 384 AA; 43861 MW; 3629D17E6A926275 CRC64;
MQDLTKNEME IKVASLNGNW KLNTPKLEKV FEFENFKEAL EFVTKVGEIA DEIQHHPDVQ
ISYGTVILNI YTHDTQGITD LDFKLAERID SLESNNDAEV LDNMDMLKNG SDFEKRKAAG
RLGNLRDERA VNLLIKALDD DDRFVQRASA RSLGKIGNEK AIKPLIRILG FVDPEFRWAA
KEALVEIGEA SEDDLISIME SKNYHQREMA IEALSEIGSE KAGISIKKAL SDGESKVRWR
AARAVSKWYD EETVNTLKEL SKKDPDRKVR DEAIKSLNIV ESMVKSLFND FEKHLDYIST
DIRSKNIKGG KSFSSPKKMF FSAHFASPYR VRFYLYQGSK GIKELEKMKG DPQWGAIYLQ
KEEDLEKVLE AVKKSYIITK KDFG
//