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Entry: A0A1C6LYV9_9BURK
LinkDB: A0A1C6LYV9_9BURK
Original site: A0A1C6LYV9_9BURK 
ID   A0A1C6LYV9_9BURK        Unreviewed;       589 AA.
AC   A0A1C6LYV9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Alcohol dehydrogenase (Cytochrome c) {ECO:0000313|EMBL:SCK11674.1};
GN   ORFNames=VAR608DRAFT_0615 {ECO:0000313|EMBL:SCK11674.1};
OS   Variovorax sp. HW608.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1034889 {ECO:0000313|EMBL:SCK11674.1, ECO:0000313|Proteomes:UP000198203};
RN   [1] {ECO:0000313|Proteomes:UP000198203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HW608 {ECO:0000313|Proteomes:UP000198203};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) 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; LT607803; SCK11674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6LYV9; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000198203; Chromosome i.
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; cd10277; PQQ_ADH_I; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR   InterPro; IPR034119; ADHI.
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; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   PANTHER; PTHR32303:SF20; QUINOPROTEIN ETHANOL DEHYDROGENASE; 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.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..589
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008740048"
FT   ACT_SITE        317
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         131
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         175
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         193
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        125..126
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   589 AA;  63228 MW;  030BA8EF6DAFB7B1 CRC64;
     MQLKLLTALI AVGLAAATAH AQVTDQMIQS EATAKGNVLT WGINTQGQRY SPLKQVNSAN
     AGKLLPVWAF SFGGEKQRGQ ESQPVIANGK MFVTASYSRI FALDAATGKK LWKYEHRLPE
     GIMPCCDVVN RGAALYDNLV IFATLDAQLV ALDQNTGDVV WKEKFDDYAA GYSATAAPLI
     ADGVLLTGVS GGEFGVVGRV EARDPRTGKL IWTRPTVEGH MGYVYDKDGN KKENGISGTV
     NKSWPGDLWK TGGATTWLGG TYDAKTGLAY FGTGNPAPWN SHLREGDNLF SCSTVAIDVK
     TGQIKWSYQG TPNDSWDFDG VNEFVTFDMD GKRVGGKADR NGFFYVNDAT TGKLINAFPF
     VKKITWASSI DLKTGRPNFI AENRPGDPTA APEGKKGSSV FAAPGFLGGK NQMPMAYSPD
     TRMFYVPANE WGMDIWNEPV AYKKGAAYLG AGFTIKPLNE DYIGSLRAID PKTGKMAWEV
     KNAAPLWGGV LTTGGNLVFW GTPEGYLKAA DAKTGKVVWQ FQTGSGIVAP PVTWMQGGEQ
     YVAVVSGWGG AVPLWGGEVA KRVNLLEQGG MVWVFKIPGA SGATRVASN
//
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