ID G3IUW5_METTV Unreviewed; 618 AA.
AC G3IUW5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:EGW21650.1};
DE Flags: Precursor;
GN ORFNames=Mettu_0419 {ECO:0000313|EMBL:EGW21650.1};
OS Methylobacter tundripaludum (strain ATCC BAA-1195 / DSM 17260 / SV96).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylobacter.
OX NCBI_TaxID=697282 {ECO:0000313|EMBL:EGW21650.1, ECO:0000313|Proteomes:UP000004664};
RN [1] {ECO:0000313|EMBL:EGW21650.1, ECO:0000313|Proteomes:UP000004664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1195 / DSM 17260 / SV96
RC {ECO:0000313|Proteomes:UP000004664};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Held B.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Ovchinnikova G., Pagani I., Klotz M.G., Dispirito A.A., Murrell J.C.,
RA Dunfield P., Kalyuzhnaya M.G., Svenning M., Trotsenko Y.A., Stein L.Y.,
RA Woyke T.;
RT "Genomic sequence of Methylobacter tundripaludum SV96.";
RL Submitted (JUN-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; JH109152; EGW21650.1; -; Genomic_DNA.
DR RefSeq; WP_006889629.1; NZ_JH109152.1.
DR AlphaFoldDB; G3IUW5; -.
DR STRING; 697282.Mettu_0419; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_0_0_6; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000004664; 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 Reference proteome {ECO:0000313|Proteomes:UP000004664};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..618
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003445495"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 81
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 135
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 179
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 265
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT DISULFID 129..130
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 618 AA; 66661 MW; 5BF61E50FFF5C4F9 CRC64;
MKKPLKSWLL ASSVAALLAA PAVSTANSDV EKLTQNPANW ATWGGDYAGT RYSKLSEINA
TNVKNLQPAW SFSTGVLRGH EGGPLVVNDV LYIHTPFPNT VYAIDQKTQS VIWEFTPTQD
ADVTIPVMCC DTVNRGLAYG DGKIFLQQSD TVLTALDAKT GKRVWSVQNG DPKLGMTNTA
APLVVKDKVL TGISGGEFGV RGFLAAYDIN TGELAWKGYS MGPDKDTLID AKKTTTWKDG
KVTPVGENSS LSTWEGDQWK IGGGTTWGWT SYDPKLNLIY YGSGNPSTWN PVQRPGDNKW
SMSLWARDAD TGAVKWVYQM TPHDEWDFDG INETVLVDQD VKGKMHKTIV HFDRNGFGYT
LDRETGELLV AEKFDKSVNW ATHVDMNTGR PQVVAKYSTQ QNGEDVNTKG VCPAALGSKN
QQPVSYSPQT GLFYISGNHL CMDYEPFEVS YTAGQPYVGA TLTMMPAGAD VLTGKPDNST
NLGQFTAYDA KTGKIAWSNK EQFSVWSGSV ATAGGVVFYG TLEGYLKAVD AKTGKELYKF
KTPSGIIGNV NTWEYNGKQY VGVLSGIGGW AGIGIAAGLD SGEEGSNSEG LGAVGAYRSL
SSYTKLGGTL TVFALPSN
//
