ID A0A252BV20_9PROT Unreviewed; 472 AA.
AC A0A252BV20;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OUJ12789.1};
GN ORFNames=HK26_12880 {ECO:0000313|EMBL:OUJ12789.1};
OS Acetobacter okinawensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1076594 {ECO:0000313|EMBL:OUJ12789.1, ECO:0000313|Proteomes:UP000194931};
RN [1] {ECO:0000313|EMBL:OUJ12789.1, ECO:0000313|Proteomes:UP000194931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DsW_060 {ECO:0000313|EMBL:OUJ12789.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR000018-50};
CC Note=Binds 3 heme c groups covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000018-50};
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:OUJ12789.1}.
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DR EMBL; JOPJ01000009; OUJ12789.1; -; Genomic_DNA.
DR RefSeq; WP_025825390.1; NZ_JOPJ01000009.1.
DR AlphaFoldDB; A0A252BV20; -.
DR STRING; 1236501.GCA_000613865_03049; -.
DR eggNOG; COG2010; Bacteria.
DR OrthoDB; 9811281at2; -.
DR Proteomes; UP000194931; Unassembled WGS sequence.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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; 3.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR PANTHER; PTHR35008:SF8; BLL4482 PROTEIN; 1.
DR PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; Cytochrome c; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022660};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000018-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000018-51};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000018-51};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022660}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..472
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011528116"
FT DOMAIN 32..135
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 179..294
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 318..408
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 46
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 49
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 50
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
FT BINDING 194
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 197
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 198
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
FT BINDING 331
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 334
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 335
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
SQ SEQUENCE 472 AA; 50326 MW; D05F9882F191B19D CRC64;
MMMNRLKAAL GAVTVGLLAG TSLAHAQGAE EDLIKKGEYV ARLGDCVACH TALNGQKFAG
GLAIKTPIGM IYSTNITPDP TYGIGTYTLQ EFDEAVRHGI RKDGSTLYPA MPYPAFSRMT
QDDVKSLYAY FMHGVQPVAQ KNREVGISWP MSMRWPLAIW RTMFAPTPKD FTPAPGTDPE
IARGEYLVTG AGHCGACHTP RGFAMQEKAL DAAGGPDFLA GGAPIDNWIA PSLRNDPVVG
LGRWSEDDLF QFLKSGRTDH SAVFGGMADV VGWSTQYFTD SDLHAIAKYL KALPPVPPSR
GDYTYDPSTA QALDSGNTAS NPGARVYVEQ CAACHRNDGG GVARMFPPLA GNSVVVTDDP
TSIAHIIVAG GVLPPTNWAP SAVAMPDYKS ILSDQQIADV VNFIRSAWGN KAPANVTAAD
VQKLRLDHAP IPTAGWADPT AATATWGLFM PQPYGSGWTF APQTHTGVDA EQ
//
