ID A0A0Q7PTE1_9GAMM Unreviewed; 592 AA.
AC A0A0Q7PTE1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Methanol dehydrogenase {ECO:0000313|EMBL:KQY54805.1};
GN ORFNames=ASD14_01070 {ECO:0000313|EMBL:KQY54805.1};
OS Lysobacter sp. Root494.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736549 {ECO:0000313|EMBL:KQY54805.1, ECO:0000313|Proteomes:UP000051738};
RN [1] {ECO:0000313|EMBL:KQY54805.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY54805.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY54805.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY54805.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQY54805.1}.
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DR EMBL; LMFH01000001; KQY54805.1; -; Genomic_DNA.
DR RefSeq; WP_056127644.1; NZ_LMFH01000001.1.
DR AlphaFoldDB; A0A0Q7PTE1; -.
DR STRING; 1736549.ASD14_01070; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000051738; Unassembled WGS sequence.
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; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 4.
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:UP000051738};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..592
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006319569"
FT ACT_SITE 318
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 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 318
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 592 AA; 64474 MW; 1C14B083609E07E1 CRC64;
MRGWRMAMLW CALCGMLPLA HAQQSSAHSP TDGEWRMPAH DYASTRYSPL AEIQRGNVKQ
LKVEFTFDTG IDHGQEAAPL VVGDTMYVVT PYPNVLFALD LSQSGKLKWK YQPKPEAAAQ
GVACCDVVNR GAVYWDGAVI YNTLDGDTVA VDASTGKERW KTKLGNIQKG ESITAAPLVV
KDKVLVGNSG GEFGVRGWLA ALDAGSGKLL WKMYATGPDA DVGIGPNFKP FYPADRGKDL
GVRTWPPQAW KIGGGTAWGW ISYDPQLDLV YYGTANPGPW NEAQRPGDNK WTAGIFARDP
DDGSARWFYQ FSPHDLYDYD AINENLLLDL RIDGQLRKTL VRPERNGFVY VMDRATGQVL
SADPFVQGNS ILRVDLKTGR PVYNPEKKTE QGKVVRGICP AAPGAKDWNP SAFSPRTGLV
YIPHINLCMD WLSVETNYIA GTPYVGAEVK MYAGPGGHRG VVTAWDPIAR TPRWIIKEDL
PVWSGALATA GDVVFYGTMD GWFKAVDART GAELWKFRTG SGVIGQPVTY RGPDGHQYVA
VLSGVGGWAG AIVVGNLDPR DKGAALGFVN ATADLKDKTQ PGGTLYVFAL PH
//
