ID B8IWZ3_METNO Unreviewed; 629 AA.
AC B8IWZ3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:ACL63034.1};
GN OrderedLocusNames=Mnod_8040 {ECO:0000313|EMBL:ACL63034.1};
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OG Plasmid pMNOD02 {ECO:0000313|EMBL:ACL63034.1,
OG ECO:0000313|Proteomes:UP000008207}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL63034.1, ECO:0000313|Proteomes:UP000008207};
RN [1] {ECO:0000313|Proteomes:UP000008207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC {ECO:0000313|Proteomes:UP000008207};
RC PLASMID=Plasmid pMNOD02 {ECO:0000313|Proteomes:UP000008207};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of plasmid 2 of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) 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; CP001351; ACL63034.1; -; Genomic_DNA.
DR AlphaFoldDB; B8IWZ3; -.
DR KEGG; mno:Mnod_8040; -.
DR HOGENOM; CLU_018478_0_0_5; -.
DR Proteomes; UP000008207; Plasmid pMNOD02.
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 SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00363; BACTERIAL_PQQ_1; 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 Plasmid {ECO:0000313|EMBL:ACL63034.1};
KW PQQ {ECO:0000256|ARBA:ARBA00022891, ECO:0000256|PIRSR:PIRSR617512-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..629
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002872016"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 86
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 140
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 190
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 206..207
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 272
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 574
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT DISULFID 134..135
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 629 AA; 68798 MW; 3DB559D8373BB0B2 CRC64;
MLGKIVVRCR TGVSVAALAA LLPLAGPSAL ANDKLVELSK SDGNWVMPGK NYDSDNYSKL
KQINAENVKN LKVSWQFSTG LLNGHEGAPL VVDGTMYVHT SFPNNTFALG LDDPGKILWQ
DKPKQNPAAR SVACCDLVNR GLAYWPGDGK TPSLILKTLL DGHVVALNAQ TGETVWKIEN
SDIRVGSTLT IAPYVVKDKV IIGSSGAELG VRGYLTAYDV RTGEQKWRAY ATGPDSDLLL
AKDFNIHNAH YGQKGLGTST WEGDAWKIGG GTNWGWYAYD PGTNLIYFGT GNPAPWNETM
RPGDNKWTMT IFARDVDTGE AKFGYQKTPH DEWDYAGVNV MMLSTQKDRS GKERKLLTHP
DRNGIVYTLD RTNGDLISAH KIDDTVNVFK TVDLKSGLPV RDPEYGTRMD HLAKDICPSA
MGYHNQGHDS YDPERKLFYM GINHICMDWE PFMLPYRAGQ FFVGATLNMY PGPKGDRQNA
EGLGQIKAYD AITGKFKWEK MERFAVWGGT LATAGNVVFY GTLDGFIKAR HSDTGELLWK
AKLPSGAIGY PVTYTHKGTQ YVAIYYGVGG WPGVGLVFDL QDPTAGLGAV GAFKKLANYT
QMGGGVTVFS LDGKGPYDDP NTGEYVAAN
//
