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Database: UniProt
Entry: J3HVK6_9BRAD
LinkDB: J3HVK6_9BRAD
Original site: J3HVK6_9BRAD 
ID   J3HVK6_9BRAD            Unreviewed;       602 AA.
AC   J3HVK6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:EJN07201.1};
GN   ORFNames=PMI42_07913 {ECO:0000313|EMBL:EJN07201.1};
OS   Bradyrhizobium sp. YR681.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1144344 {ECO:0000313|EMBL:EJN07201.1, ECO:0000313|Proteomes:UP000007272};
RN   [1] {ECO:0000313|EMBL:EJN07201.1, ECO:0000313|Proteomes:UP000007272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR681 {ECO:0000313|EMBL:EJN07201.1,
RC   ECO:0000313|Proteomes:UP000007272};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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}.
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:EJN07201.1}.
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DR   EMBL; AKIY01000328; EJN07201.1; -; Genomic_DNA.
DR   RefSeq; WP_008144226.1; NZ_AKIY01000328.1.
DR   AlphaFoldDB; J3HVK6; -.
DR   PATRIC; fig|1144344.3.peg.7110; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000007272; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; 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   InterPro; IPR001479; Quinoprotein_DH_CS.
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; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 6.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 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|ARBA:ARBA00022891, ECO:0000256|PIRSR:PIRSR617512-2};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..602
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003769182"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         78
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         132
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         176
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         320
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   DISULFID        126..127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   602 AA;  64814 MW;  254D8CC6E36E28CF CRC64;
     MRKVLLATFL GSAAALAVGG ASANDELNKM AQNPKDWVMP TGDYANTRYS KLNQINAQNV
     GKLQVAWTFS TGVLRGHEGG PLIIGNMMYV HTPFPNKVYA IDLSNENKIV WKYEPKQDPN
     VIPVMCCDTV NRGLAFGDGK IFLHQADTTL VALDAKTGQV AWTAKNGDPG KGETGTSAPM
     VVKDKVLIGI SGGEFGVQAH MSAYDIKTGK LAWRGYSEGP DDQILVDAEK TTALGKPVGK
     DSSLKTWQGD QWKIGGGATW GWISYDPELN LVYYGSGNPS TWNPKQRPGD NKWSMTIWAR
     NPDTGQAKWV YQMTPHDEWD YDGVNEMILS DQAINGQPRK LLTHFDRNGL GYTLDRGTGE
     LLVAEKYDPK VNWTSGVDMD KNSPTYGRPK VLDAASTDKA GEDHNVKGIC PAALGTKDEQ
     PAAYSPDTQL FYVPTNHVCM DYEPFKVSYT AGQPYVGATL SMYPPAGETH MGNFIAWDGK
     TGKIVWSNKE QFSVWSGALA TAGNVVFYGT LEGYLKAVDA KTGKELYKFK TPSGIIGNVT
     TYENGGKQYV AVLSGVGGWA GIGLAAGLTD PTAGLGAVGG YAALSNYTAL GGTLTVFSLP
     AN
//
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