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Database: UniProt
Entry: H5YQI3_9BRAD
LinkDB: H5YQI3_9BRAD
Original site: H5YQI3_9BRAD 
ID   H5YQI3_9BRAD            Unreviewed;       601 AA.
AC   H5YQI3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:EHR04815.1};
GN   ORFNames=Bra471DRAFT_05620 {ECO:0000313|EMBL:EHR04815.1};
OS   Bradyrhizobium sp. WSM471.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR04815.1};
RN   [1] {ECO:0000313|EMBL:EHR04815.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM471 {ECO:0000313|EMBL:EHR04815.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; CM001442; EHR04815.1; -; Genomic_DNA.
DR   RefSeq; WP_007612979.1; NZ_CM001442.1.
DR   AlphaFoldDB; H5YQI3; -.
DR   HOGENOM; CLU_018478_0_0_5; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000005774; Chromosome.
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..601
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003602673"
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   601 AA;  64897 MW;  FCB5E495939E9811 CRC64;
     MRKVLLAAYL GSAAALAVGS ASANDEVLKM SQNPKDWVMP TGDYANTRYS KLNQINAQNV
     GKLQVAWTFS TGVLRGHEGG PLIIGNMMYV HTPFPNKVYA IDLSNENKIV WKYEPKQDPN
     VIPVMCCDTV NRGLAYGDGK IFLHQADTTL VALDAKSGQV AWTAKNGDAS KGETGTSAPM
     VVKDKVLIGI SGGEFGVQAH MTAYDIKTGK LAWRGYSEGP DDQILVDAEK TTALGKPIGK
     DSSLKTWQGD QWKIGGGATW GWISYDPELN LVYYGSGNPS TWNPKQRPGD NKWSMTIWAR
     NPDTGKAKWV YQMTPHDEWD YDGVNEMILS DQSINGQPRK LLTHFDRNGL GYTLDRATGE
     LLVAEKYDPK VNWTSGVDMD KNSPTYGRPK VLDSASTDKA GEDHNVKGIC PAALGTKDEQ
     PAAYSPDTQL FYVPTNHVCM DYEPFKVSYT AGQPYVGATL SMYPPQGETH MGNFIAWDGK
     TGKIVWSNKE QFSVWSGALA TAGNVVFYGT LEGYLKAVDA KTGKELYKFK TPSGIIGNVT
     TYENGGKQYV AVLSGVGGWA GIGLAAGLTD PTAGLGAVGG YAALSNYTAL GGTLTVFSLP
     N
//
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