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Database: UniProt
Entry: D8JZ70_HYPDA
LinkDB: D8JZ70_HYPDA
Original site: D8JZ70_HYPDA 
ID   D8JZ70_HYPDA            Unreviewed;       607 AA.
AC   D8JZ70;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:ADJ23672.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Hden_1869 {ECO:0000313|EMBL:ADJ23672.1};
OS   Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS   TK 0415).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ23672.1, ECO:0000313|Proteomes:UP000002033};
RN   [1] {ECO:0000313|Proteomes:UP000002033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC   {ECO:0000313|Proteomes:UP000002033};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR617512-3};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR617512-3};
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000256|PIRSR:PIRSR617512-2};
CC       Note=Binds 1 PQQ group per subunit. {ECO:0000256|PIRSR:PIRSR617512-2};
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008156}.
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DR   EMBL; CP002083; ADJ23672.1; -; Genomic_DNA.
DR   RefSeq; WP_013215831.1; NC_014313.1.
DR   AlphaFoldDB; D8JZ70; -.
DR   STRING; 582899.Hden_1869; -.
DR   KEGG; hdn:Hden_1869; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_0_0_5; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000002033; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   CDD; cd10278; PQQ_MDH; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   NCBIfam; TIGR03075; PQQ_enz_alc_DH; 1.
DR   PANTHER; PTHR32303:SF22; METHANOL DEHYDROGENASE LARGE SUBUNIT-LIKE PROTEIN; 1.
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   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR617512-3};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR617512-4};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR617512-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   PQQ {ECO:0000256|PIRSR:PIRSR617512-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002033};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..607
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003116386"
FT   ACT_SITE        324
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         76
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         130
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         174
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         190..191
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         256
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         276
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   DISULFID        124..125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   607 AA;  65599 MW;  7E6935EB23827889 CRC64;
     MRKLMFAASV AAAALASPAL ANDDVVKNQA NPNFWASQSG DYAATRYSTL DQINTSNVAD
     LKVAWTFSTG VLRGHEGSPL VIGDVMYLHT PFPNIVFALN LADEQKIIWK YEPKQDPSVI
     PVMCCDTVNR GLAYADGKII LQQADTNVVA LDAKTGKELW KVANGDPKRG ETATNTVLIV
     RDKVITAISG AEFGVRGYVT AYDLNTGKLA WRAYNIGPDN EILFDPNKTT SLGKPVGKDS
     SLKTWNGDQW KIGGGTLWGG WSYDPEADLF YYGSANPSTW NPSQRAGPDG KPIDQKWTMA
     IIARNPDTGV ASWAYQMTPF DEWDYDGVNE NILVDLDIKG QKTPALVHFD RNGFAYTLNR
     KNGELLVAEK FDPVVNWATG IDMDKASPNY GRPIRVAKYS TFRDGKGADF NTKGICPAAL
     GSKDMQPASF SKLTGLFYVP TNHVCMDYEP FKVSYTSGQP YVGATLSMFP APDSHGGMGN
     FIAWDASQGK IVWSKPEQFS VWSGALTTAG GVVFYGTLEG YFKAVDQKDG KELFKFKTPS
     GIISNAMTYT HGGKQYVGVM SGVGGWAGIG LAAGLTNPND GLGAVGGYAG LKQYTNLGGT
     LTVFSLP
//
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