PDL2_ARATH
ID PDL2_ARATH Reviewed; 187 AA.
AC Q6QJ72; Q8GZ70;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Pterin-4-alpha-carbinolamine dehydratase 2, mitochondrial {ECO:0000305};
DE EC=4.2.1.96 {ECO:0000305|PubMed:18245455};
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase {ECO:0000305};
DE AltName: Full=PCD/DCoH-like protein 2 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=PDL2 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At1g29810 {ECO:0000312|Araport:AT1G29810};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Plume A.M.;
RT "Functional characterisation of Arabidopsis DRGs: clues from the DRG2
RT interactor PDL1.";
RL Thesis (2002), University of Queensland, Australia.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18245455; DOI=10.1104/pp.107.114090;
RA Naponelli V., Noiriel A., Ziemak M.J., Beverley S.M., Lye L.F., Plume A.M.,
RA Botella J.R., Loizeau K., Ravanel S., Rebeille F., de Crecy-Lagard V.,
RA Hanson A.D.;
RT "Phylogenomic and functional analysis of pterin-4a-carbinolamine
RT dehydratase family (COG2154) proteins in plants and microorganisms.";
RL Plant Physiol. 146:1515-1527(2008).
CC -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis (By similarity).
CC Possesses pterin-4-alpha-carbinolamine dehydratase activity when
CC expressed in a bacterial heterolgous system (PubMed:18245455).
CC {ECO:0000250|UniProtKB:P61457, ECO:0000269|PubMed:18245455}.
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:0000305|PubMed:18245455};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18245455}.
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY536641; AAS45834.1; -; mRNA.
DR EMBL; AC008030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE31133.1; -; Genomic_DNA.
DR EMBL; AK117179; BAC41856.1; -; mRNA.
DR EMBL; BT003720; AAO39948.1; -; mRNA.
DR RefSeq; NP_174274.2; NM_102721.3.
DR AlphaFoldDB; Q6QJ72; -.
DR SMR; Q6QJ72; -.
DR STRING; 3702.AT1G29810.1; -.
DR MetOSite; Q6QJ72; -.
DR PaxDb; Q6QJ72; -.
DR PRIDE; Q6QJ72; -.
DR EnsemblPlants; AT1G29810.1; AT1G29810.1; AT1G29810.
DR GeneID; 839859; -.
DR Gramene; AT1G29810.1; AT1G29810.1; AT1G29810.
DR KEGG; ath:AT1G29810; -.
DR Araport; AT1G29810; -.
DR TAIR; locus:2019297; AT1G29810.
DR eggNOG; KOG4073; Eukaryota.
DR HOGENOM; CLU_081974_0_0_1; -.
DR InParanoid; Q6QJ72; -.
DR OrthoDB; 1588292at2759; -.
DR PhylomeDB; Q6QJ72; -.
DR PRO; PR:Q6QJ72; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6QJ72; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IDA:UniProtKB.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.20; -; 1.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR001533; Pterin_deHydtase.
DR PANTHER; PTHR12599; PTHR12599; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; SSF55248; 1.
PE 1: Evidence at protein level;
KW Lyase; Mitochondrion; Reference proteome; Tetrahydrobiopterin biosynthesis;
KW Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..187
FT /note="Pterin-4-alpha-carbinolamine dehydratase 2,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000443386"
FT CONFLICT 128
FT /note="A -> T (in Ref. 4; BAC41856 and 5; AAO39948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 187 AA; 21063 MW; 61167C49F32F8F0E CRC64;
MSRLLLPKLF SISRTQVPAA SLFNNLYRRH KRFVHWTSKM STDSVRSSTT GGSASGARTF
CSLADLSTKK CVPCNAKDLR AMTEQSAQDL LQKVAGWDLA NDNDTLKLHR SWRVKSFTKG
LDFFQRVADI AESEGHHPDL HLVGWNNVKI EIWTHAIGGL TENDFILAAK INELQVEDLL
RKKKVAK
