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Database: UniProt
Entry: X7F792_9RHOB
LinkDB: X7F792_9RHOB
Original site: X7F792_9RHOB 
ID   X7F792_9RHOB            Unreviewed;       599 AA.
AC   X7F792;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Methanol dehydrogenase {ECO:0000313|EMBL:ETX27944.1};
GN   ORFNames=RISW2_10770 {ECO:0000313|EMBL:ETX27944.1};
OS   Roseivivax isoporae LMG 25204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX27944.1, ECO:0000313|Proteomes:UP000023430};
RN   [1] {ECO:0000313|EMBL:ETX27944.1, ECO:0000313|Proteomes:UP000023430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX27944.1,
RC   ECO:0000313|Proteomes:UP000023430};
RA   Lai Q., Li G., Shao Z.;
RT   "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL   Submitted (JAN-2014) 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:ETX27944.1}.
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DR   EMBL; JAME01000025; ETX27944.1; -; Genomic_DNA.
DR   RefSeq; WP_043773054.1; NZ_JAME01000025.1.
DR   AlphaFoldDB; X7F792; -.
DR   STRING; 1449351.RISW2_10770; -.
DR   PATRIC; fig|1449351.3.peg.3211; -.
DR   eggNOG; COG4993; Bacteria.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000023430; 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; PF13360; PQQ_2; 1.
DR   Pfam; PF13570; PQQ_3; 1.
DR   SMART; SM00564; PQQ; 5.
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:UP000023430};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..599
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004980141"
FT   ACT_SITE        317
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         75
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         129
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         173
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         191
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         255
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         275
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         317
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   DISULFID        123..124
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   599 AA;  65303 MW;  926A43DFB6DAAE95 CRC64;
     MKRLTLLTSG LALVAGMAAA NDDLITQMDN ADQWAIQTGD YKNQRYSELD QINAENVGDL
     QVAWTFSTGV LRGHEGSPLV IGDTMYLHTP FPNIVYALDL ANDGKIKWKY EPQQDPDVIP
     VMCCDTVNRG VAYADGKIFL HQADTTVVAL NAESGEVMWE VVNGDPSKGE TNTATVLPVK
     DKVIVGISGG EFGVRGSVTA YDMNTGEQVW RAYSMGPDED ILVDPENTTH LGEPVGENSG
     TNTWEGDQWM IGGGTTWGWY SADMDENLFY YGTGNPSTWN PSQRPGDNRW SMTVMARDID
     TGMAKWFYQM TPHDEWDYDG VNEMILTEQE IDGEERKLLT HFDRNGLAYT MDRVSGELLV
     AEKYDPAVNW TTGVDMDPES DTYGRPAVVA QYSTEQQGED VNTTGICPAA LGTKDQQPAA
     YSPKTETFYV PTNHVCMDYE PFRVSYTAGQ PYVGATLAMY PAPDSHGGMG NFIAWDNING
     EIKWSIPEQF SVWSGALATA GDVVFYGTLE GYLKAVHAET GDELYRFKTP SGIIGNVMTY
     MHEGKQHIGI LSGVGGWAGI GLAAGLTNPN DGLGAVGGYA ALSDYTALGG QLTVFTLPD
//
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