ID A0A0A5GI65_9BACI Unreviewed; 769 AA.
AC A0A0A5GI65;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Quinoprotein ethanol dehydrogenase {ECO:0000313|EMBL:KGX91704.1};
GN ORFNames=N783_00010 {ECO:0000313|EMBL:KGX91704.1};
OS Pontibacillus marinus BH030004 = DSM 16465.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX91704.1, ECO:0000313|Proteomes:UP000030403};
RN [1] {ECO:0000313|EMBL:KGX91704.1, ECO:0000313|Proteomes:UP000030403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030004 {ECO:0000313|EMBL:KGX91704.1,
RC ECO:0000313|Proteomes:UP000030403};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000256|ARBA:ARBA00001931};
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:KGX91704.1}.
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; AVPF01000001; KGX91704.1; -; Genomic_DNA.
DR RefSeq; WP_051254958.1; NZ_AVPF01000001.1.
DR AlphaFoldDB; A0A0A5GI65; -.
DR STRING; 1385511.GCA_000425225_00252; -.
DR eggNOG; COG2010; Bacteria.
DR eggNOG; COG4993; Bacteria.
DR Proteomes; UP000030403; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
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 Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030403};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 688..764
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 35..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 84381 MW; BF94F980A421726C CRC64;
MSTSQKVYWG IVLVVVVFLF GLIIYEYANF TSQSSSVSST EKGSKTETTP EKQEGTESET
KDDDKISDEE TTQDQPESTS TQNESVEKND QPTITQHRTY NGKTAPAFTP EDLTALPTSN
WLTNGGDTYN RRYSPLNEIN ADNVQKLKGE WVAALGSGTE FKYSGEATPI VYDGVMYVIT
GANDVLALDA KSGETIWEFR ANLSEKLDTV CCGWTSRGVA IGDGKVYVGL LDARLVALDQ
KTGEIVWETT VADWEKGYTI TNAPLYYDGK VYTGLSGGEY GIRGRVTAFD ADMGREIWRF
YTIPGPGEEG YDTWPHDNDA WLKGGAPVWQ TPAVDPELGT LYFSTGNAAP DLDGSQREGN
NLFTSSIVAI DVNTGKYKWH FQEVHHDIWD LDAPNPVILF DVEKDGETRK ALAQAGKTGW
VYILDRVTGE PLIGIEEKAV PQDPRQKTAA TQPIPKGDSF VPQDISEEDV KRDLGEFEGE
YGDIFTPFWE EPVALKPSAF GGANWPPSAY NPNTEYFYVL GTDSYMTYTR SEEEFEEGSD
YMGSIMAPVN DAPEHGTVTA IDVKTNKIAW QKVWDDKAYS GVLTTKGNLV FVGHNDGRFI
AYHAETGETL WEFKADAGAN APAITYELDG KQYIAILVAG NSLAGSKHGD SLWTFSLDGT
IESGETPERI SAEATSTSKE TQGKETPDQV ASGEEIYKTN CLSCHGTEGA NGHNGPNLQN
SAITENMEKI IERINNGGSK MPAFKGTLTE QEIQDVARYL NEVVAPKGE
//
