ID   A0A2A5QTY5_9EURY        Unreviewed;       625 AA.
AC   A0A2A5QTY5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:PCR90229.1};
GN   ORFNames=CP557_06545 {ECO:0000313|EMBL:PCR90229.1};
OS   Natrinema ejinorense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=373386 {ECO:0000313|EMBL:PCR90229.1, ECO:0000313|Proteomes:UP000219689};
RN   [1] {ECO:0000313|EMBL:PCR90229.1, ECO:0000313|Proteomes:UP000219689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13890 {ECO:0000313|EMBL:PCR90229.1,
RC   ECO:0000313|Proteomes:UP000219689};
RA   Roh S.W., Kim Y.B., Kim J.Y.;
RT   "Genome sequences of Natrinema ejinorence JCM 13890T.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000256|ARBA:ARBA00001931};
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008156}.
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:PCR90229.1}.
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DR   EMBL; NXNI01000001; PCR90229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5QTY5; -.
DR   OrthoDB; 8638at2157; -.
DR   Proteomes; UP000219689; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 2.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 3.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..507
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  69254 MW;  71D32EE4C1121AF4 CRC64;
     MTYESHLIDL PEDAPWNEKP GESVVEQGDI DQIPERDVTE EDLAATGEEP TNWLIMGGSY
     QSQRHTTADV ITPENVDQLE AEYRLEVADD PNDFQGSPII VDGDPPIMYT TVGPDLLYAI
     NARTGDLLWT HFYEPVVGAS DETPPAERGP AVLGDTVYKS TLDLGVIAID RYTGEERWYY
     NGAAAYRGEV ADDVMHEELQ WERSRGTTSS FPPLIYDGML MKGSFGGEFG VSGFFDAIDL
     EGNPQWRVNM TPEHEWVGDS WEHGGATAWA SGAVEPDEGT VVIPSANPGP WYGTVRPGYN
     PYSCGKVAVN VEDGEYQWHH QDSPHDWWDY DSPSPPVLFE AEVEGETRQF ATWPGKTGWV
     YTVDMETGQL HQRSDEYVQH LNMFSLPPYD DLESAPWIMP DLIGGTNPQP SAYDPETRTL
     VVKGTNYPIK FSWFEVEYAA GETYIGMDTV RKTEPADAEE GEQREGDETP DENGDGGDEL
     HEEEQERDEE EEEEEEEEEE TQQFENEEVP EWNEMAGVIA GIDPLTGEVK WQNWFSWEAG
     PPWGGSLTTA TGVAFAGGPT GQLHAFDTET GEHLAAHEVG DHGVDGAPAS WYDPAEGKQY
     VAIPGGGGNQ VDEEGNTIAV FSLEE
//