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}.
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; 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
//