ID A0A0F6A1W2_9GAMM Unreviewed; 602 AA.
AC A0A0F6A1W2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Methanol dehydrogenase {ECO:0000313|EMBL:KKD61948.1};
GN ORFNames=RN22_03330 {ECO:0000313|EMBL:KKD61948.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD61948.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD61948.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD61948.1,
RC ECO:0000313|Proteomes:UP000033732};
RA Adrian T.-G.-S., Chan K.-G.;
RT "Genome sequencing of Grimontia sp. AD028.";
RL Submitted (APR-2015) 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}.
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:KKD61948.1}.
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DR EMBL; LASY01000014; KKD61948.1; -; Genomic_DNA.
DR RefSeq; WP_046303073.1; NZ_LASY01000014.1.
DR AlphaFoldDB; A0A0F6A1W2; -.
DR PATRIC; fig|1581149.3.peg.718; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000033732; 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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..602
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002498725"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 84
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 137
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 181
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 263
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT DISULFID 131..132
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 602 AA; 65751 MW; 168D4D872DF2ED40 CRC64;
MIGAVRLRRC LAAVATLSLT LLFPAASQAN DELIKLQEDP NQWVMWGGDY SGTRYSPLNQ
INAENAKNLQ VAWTFSTGVL RGHEGGPLVL GDTMYIHTPF PNKVFAIDLK TKALKWEYEP
KQDSSVIAVM CCDTVNRGLA YADGKIFLQQ ADTTLVALDQ NTGKVVWKVV NGDPKVGATN
TNAPLVVKDK IITGISGGEF GVRGYLTAYN IKDGSVAWRA YSTGPDEEML VDPEKTTEML
KPIGKDSSLE SWEGDQWKIG GGTTWGWFSY DPELNLIYYG TGNPSTWNPS QRPGDNKYSM
TIMARDADTG MAKWLYQMTP HDEWDYDGVN EMILVDKKFK GKDRKLLVHF DRNGFGYTLD
RETGELLVAE KFDPAVNWAT HVDMETGRPQ VVAKYSTAQN GEDVDTKGIC PAALGSKDQQ
PATYSPRTGL FYVPTNHVCM NYEPFEVSYT AGQPYVGATL SMFPAPDSHG GLGNFIAWDA
EKGEIVWSLP EPFSVWSGAL ATGGGVVFYG TLEGYLKAVD EKTGKELYRF KTPSGIIGNV
NTYMHDGKQY VAVLSGIGGW AGIGMAAGLE GDTDGLGAVG AYRKLSDYTQ LGGVLTVFAL
PN
//
