DPDH_PYRIL
ID DPDH_PYRIL Reviewed; 363 AA.
AC A1RVM8; Q8U4S7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=D-proline dehydrogenase;
DE Short=D-Pro DH;
DE Short=D-Pro dehydrogenase;
DE EC=1.5.99.13;
GN Name=dpdh; OrderedLocusNames=Pisl_1862;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-28, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RX PubMed=11823469; DOI=10.1074/jbc.m112272200;
RA Satomura T., Kawakami R., Sakuraba H., Ohshima T.;
RT "Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon
RT Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase.";
RL J. Biol. Chem. 277:12861-12867(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18558115; DOI=10.1016/j.aca.2008.04.063;
RA Tani Y., Tanaka K., Yabutani T., Mishima Y., Sakuraba H., Ohshima T.,
RA Motonaka J.;
RT "Development of a D-amino acids electrochemical sensor based on
RT immobilization of thermostable D-proline dehydrogenase within agar gel
RT membrane.";
RL Anal. Chim. Acta 619:215-220(2008).
CC -!- FUNCTION: Catalyzes the dehydrogenation of D-proline. Can also use
CC other D-amino acids, but with lower efficiency.
CC {ECO:0000269|PubMed:11823469, ECO:0000269|PubMed:18558115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + D-proline = 1-pyrroline-2-carboxylate + AH2;
CC Xref=Rhea:RHEA:27306, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:39785, ChEBI:CHEBI:57726; EC=1.5.99.13;
CC Evidence={ECO:0000269|PubMed:11823469, ECO:0000269|PubMed:18558115};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11823469};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 mM for D-proline {ECO:0000269|PubMed:11823469};
CC KM=9.5 mM for allo-4-hydroxy-D-proline {ECO:0000269|PubMed:11823469};
CC pH dependence:
CC Optimum pH is 7.5. Half of activity at pH 6.5 and 8.5.
CC {ECO:0000269|PubMed:11823469};
CC Temperature dependence:
CC Optimum temperature is above 70 degrees Celsius.
CC {ECO:0000269|PubMed:11823469};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11823469}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11823469};
CC Peripheral membrane protein {ECO:0000269|PubMed:11823469}.
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR EMBL; AB071692; BAB88883.1; -; Genomic_DNA.
DR EMBL; CP000504; ABL89010.1; -; Genomic_DNA.
DR RefSeq; WP_011763585.1; NC_008701.1.
DR AlphaFoldDB; A1RVM8; -.
DR SMR; A1RVM8; -.
DR STRING; 384616.Pisl_1862; -.
DR PRIDE; A1RVM8; -.
DR EnsemblBacteria; ABL89010; ABL89010; Pisl_1862.
DR GeneID; 4618108; -.
DR KEGG; pis:Pisl_1862; -.
DR eggNOG; arCOG00758; Archaea.
DR HOGENOM; CLU_753592_0_0_2; -.
DR OMA; KGYGFRT; -.
DR OrthoDB; 60559at2157; -.
DR BioCyc; MetaCyc:MON-15358; -.
DR BRENDA; 1.5.99.13; 5240.
DR Proteomes; UP000002595; Chromosome.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Flavoprotein; Membrane;
KW Oxidoreductase.
FT CHAIN 1..363
FT /note="D-proline dehydrogenase"
FT /id="PRO_0000424074"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 363 AA; 40341 MW; 2A3FA571EABDC009 CRC64;
MKVAIVGGGI IGLFTAYHLR QQGADVVIIE QGEPGGWSKA AAGILEFTRF VINRINVRSY
PKRYLSMALR GDARIKTWDW RWISAYLRAW GREPTQDMWE AIKTLGEYSW RQYRALAEAE
NDFAYSEEPL YEVGIDVAAA LEEAKRDPLS PKVETGRCCG REALVYLDAA KLSTEDFVAR
MLRELQGVQM VRRRAQEVAG REVWLEGGDV VKADAVVVAA GYWARKFGIP VAPFKGYGFR
TTAKAQSMFI EMTKGVAVVP LPKWTKVTGR FDLDGTEDHS PSARVLQRAR EVLGNFEVLD
MSVGYRPCTP DGFPIVDKVG EVVIVTGACR LGWTYGPALG KLAADLALGK PGVEALTARR
FRR
