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Database: UniProt
Entry: A0A1M4UZ86_9RHOB
LinkDB: A0A1M4UZ86_9RHOB
Original site: A0A1M4UZ86_9RHOB 
ID   A0A1M4UZ86_9RHOB        Unreviewed;       587 AA.
AC   A0A1M4UZ86;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Alcohol dehydrogenase (Cytochrome c) {ECO:0000313|EMBL:SHE61979.1};
GN   ORFNames=SAMN05444273_10273 {ECO:0000313|EMBL:SHE61979.1};
OS   Litoreibacter ascidiaceicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Litoreibacter.
OX   NCBI_TaxID=1486859 {ECO:0000313|EMBL:SHE61979.1, ECO:0000313|Proteomes:UP000184144};
RN   [1] {ECO:0000313|EMBL:SHE61979.1, ECO:0000313|Proteomes:UP000184144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100566 {ECO:0000313|EMBL:SHE61979.1,
RC   ECO:0000313|Proteomes:UP000184144};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQUV01000002; SHE61979.1; -; Genomic_DNA.
DR   RefSeq; WP_073140767.1; NZ_FQUV01000002.1.
DR   AlphaFoldDB; A0A1M4UZ86; -.
DR   STRING; 1486859.SAMN05444273_10273; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000184144; 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; 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   InterPro; IPR001479; Quinoprotein_DH_CS.
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; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 7.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..587
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013313566"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         80
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         130
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         174
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         269
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         320
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         414..415
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   DISULFID        124..125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   587 AA;  63756 MW;  C8E7F38A97D3BCBE CRC64;
     MNRFVMAVTA AVLATGVAHA EVTEEMLLND TASTGDVLTN GMGRHLQRYS PLETLNKDNV
     KNLVPAWAFS LGGEKQRGQE TQPLVHDGVM YITGSYSRMY AIDIKTGKEI WQYDARLPEG
     ILPCCDVVNR GAAIFGDNIY FGTLDARMVA LNAKTGDVVW NKKIADYKAG YSYTAAPLIV
     RGLVITGNSG GEFGIVGEVQ ARDAETGDLV WTRPVIEGHM GTLNGEESTM TGELNATWPG
     DMWKTGGGAT WLGGSYDADT DTLVFGAGNP APWNSHLRNA GTPVEGNKGD NLYAASRIGI
     DPATGEIKWH YQTTPREGWD YDGVNEVVAY TDRSDNKRWA TADRNGFFYV LNREDGKFVS
     AVPFVKDITW AEGIDDTGRP IFIEEGRPGD PTAAADGKKG EVVFASPSFL GGKNWMPMAH
     SPKTGLFYVP SNEWGMDIWN EPITYKKGAA YLGSGFTIKP NYEDHIGSLK AIDPDTGEIK
     WEFKNDAPLW GGVMTTAGGL VFTGTPEGNF IAFDDETGEE LWSFQTGSGI VGQPITWEQD
     GEQYVTVISG WGGAVPLWGG EVAKKVNYLN QGGLLWTFRL PAQLAAK
//
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