ID B8KYK8_9GAMM Unreviewed; 722 AA.
AC B8KYK8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Alcohol dehydrogenase (Acceptor) {ECO:0000313|EMBL:EED34293.1};
GN ORFNames=NOR51B_230 {ECO:0000313|EMBL:EED34293.1};
OS Luminiphilus syltensis NOR5-1B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Luminiphilus.
OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED34293.1, ECO:0000313|Proteomes:UP000004699};
RN [1] {ECO:0000313|Proteomes:UP000004699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX PubMed=23705883;
RA Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT halotolerans.";
RL BMC Microbiol. 13:118-118(2013).
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=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR617512-2};
CC Note=Binds 1 heme c group per subunit. {ECO:0000256|PIRSR:PIRSR617512-
CC 2};
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; DS999411; EED34293.1; -; Genomic_DNA.
DR RefSeq; WP_009019041.1; NZ_DS999411.1.
DR AlphaFoldDB; B8KYK8; -.
DR STRING; 565045.NOR51B_230; -.
DR eggNOG; COG2010; Bacteria.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_0_1_6; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000004699; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR CDD; cd10279; PQQ_ADH_II; 1.
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; 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 SMART; SM00564; PQQ; 5.
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, ECO:0000256|PIRSR:PIRSR617512-3};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR617512-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR617512-3};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004699};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 634..712
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 163
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 223..224
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 282
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 374
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 647
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 650
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 651
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 690
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
SQ SEQUENCE 722 AA; 78341 MW; A727822C1AE81AFB CRC64;
MLILIKRHKS GSQLRLQSSR ISGATRPFCL AVIAKLLTFT IFCNFSVAHA DSEGATYSAT
ILSDLSDGAN WPAFGRTYGE QHFSPLKVIN RGSVSELSLD WFFDLPKGNS VTGPLQIDGK
LFFAPGYSEV HALDSVTGQL LWTFDAKAAE RAGYKLRQGW GSRGLGWWNG KIYTGTQDGR
LIAIDADTGK EVWSVMTVDP DDMRYISGPP RAFNGKVIIG HGGADAGNVR GYVTAYDAET
GQRLWRFYTV PGNPADGFEN DAMRMAAKTW AGEWWRFGGG GTVWNAITYD EQLDQIYLGT
GNGAPWNHTI RSKGEGDNLF LSSIVALNAE SGKYIWHYQT NPGETWDYNA AMDMQLAELE
IAGAPRKVLM TAPKNGFFYV IDRVDGKLIS AENIVPVTWA TDIDLNTGRP NEVPGIRYQE
GEPVAVAPSP MGAHTWLPMA YNPDERLVYI PTIELTAVFQ DFAGNKEDWE RLPNNVLDTG
AVVGYPPDTT GSSSLVAIDP VTQGQVWRLK TPGYWNGGVL TTAGGVVFQG HIDGSFNAFD
ASSGSLLWKF DAKAPVLAPP ITYRAGGRQY VTVLTGMGTS GGYLGALIEG FNLQPKKQKR
RVLTFSLGGQ AKLPVQDNAE TPLLSDDTLE TQPETLAKGH AVYAQYCAVC HGQKAIAVGA
ASDLRRSDTL KSPSAFAAVV RNGVLVDLGM PEFSDLSEES VEAVRHYVSD RAAKDRAALS
GD
//
