ID H8GK57_METAL Unreviewed; 612 AA.
AC H8GK57;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:EIC29181.1};
GN ORFNames=Metal_1395 {ECO:0000313|EMBL:EIC29181.1};
OS Methylomicrobium album BG8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomicrobium.
OX NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC29181.1, ECO:0000313|Proteomes:UP000005090};
RN [1] {ECO:0000313|EMBL:EIC29181.1, ECO:0000313|Proteomes:UP000005090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG8 {ECO:0000313|EMBL:EIC29181.1,
RC ECO:0000313|Proteomes:UP000005090};
RX PubMed=23580712;
RA Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., Op den Camp H.J.,
RA Vuilleumier S., Bringel F., Dispirito A.A., Murrell J.C., Bruce D.,
RA Cheng J.F., Copeland A., Goodwin L., Hauser L., Lajus A., Land M.L.,
RA Lapidus A., Lucas S., Medigue C., Pitluck S., Woyke T., Zeytun A.,
RA Stein L.Y.;
RT "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph
RT Methylomicrobium album Strain BG8.";
RL Genome Announc. 1:E0017013-E0017013(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001475; EIC29181.1; -; Genomic_DNA.
DR RefSeq; WP_005370874.1; NZ_CM001475.1.
DR AlphaFoldDB; H8GK57; -.
DR STRING; 686340.Metal_1395; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_0_0_6; -.
DR Proteomes; UP000005090; 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; PF13360; PQQ_2; 1.
DR Pfam; PF13570; PQQ_3; 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:UP000005090};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..612
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003612003"
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 612 AA; 66007 MW; 712F15D13F1B0BA2 CRC64;
MKKPIKSWLL ASSVAAILAA PAIASANSEL EQLSQNPANW SMWGGNYAGT RYSELSQINA
GNVKNLQPAW SFSTGVLRGH EGGPLVVNDV LYIHTPFPNT VFAIDQKTQA IIWEYTPTQD
ADVTVPVMCC DTVNRGLAYG DGKIFLQQSD TVLTALDAKT GKRVWSVQNG DPKLGMTNTQ
SPLVVKDKVL TGISGGEFGV RGFLAAYDIK TGQLAWKGYS MGPDADTLID PNKTTAWKDG
KVQPVGPNSS TSTWEGDQWK IGGGTTWGWY SYDPKLNLVY YGSGNPSTWN PAQRPGDNKW
SMSLWARDAD TGAVKWVYQM TPHDEWDYDG INETVLVDQE VKGKPHKTIV HFDRNGFGYT
LDRETGELLV AEKFDKSVNW ATHIDMHTGR PVGDPKYSTE HNGEDVTTEG ACPAALGAKN
MAPTSYSPQT GLFYISGNHL CMNYEPFEVS YTAGQPYVGA TLTMMPAGAD VITGQPDGST
NLGQFTAWDA KTGKIVWSNK EPFSVWSGSL ATAGGVVFYG TLEGYLKAVD AKTGQELYRF
KTPSGIIGNV NTWSYNGKQY IGVLSGIGGW AGIGIAAGLE GESEGLGAVG AYRSLSSFTK
LGGTLTVFTL PD
//
