ID A0A317E8S9_9PROT Unreviewed; 681 AA.
AC A0A317E8S9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:PWR22982.1};
GN ORFNames=DKG74_10055 {ECO:0000313|EMBL:PWR22982.1};
OS Zavarzinia aquatilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Zavarziniaceae; Zavarzinia.
OX NCBI_TaxID=2211142 {ECO:0000313|EMBL:PWR22982.1, ECO:0000313|Proteomes:UP000245461};
RN [1] {ECO:0000313|EMBL:PWR22982.1, ECO:0000313|Proteomes:UP000245461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AS {ECO:0000313|EMBL:PWR22982.1,
RC ECO:0000313|Proteomes:UP000245461};
RA Lee Y., Jeon C.O.;
RT "Zavarzinia sp. HR-AS.";
RL Submitted (MAY-2018) 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=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}.
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:PWR22982.1}.
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DR EMBL; QGLE01000005; PWR22982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317E8S9; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000245461; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 InterPro; IPR001479; Quinoprotein_DH_CS.
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; PS00364; BACTERIAL_PQQ_2; 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 ECO:0000256|PIRSR:PIRSR617512-4};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR617512-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR617512-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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 Reference proteome {ECO:0000313|Proteomes:UP000245461};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 592..670
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT ACT_SITE 311
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 128
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 172
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 188..189
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 338
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 398..399
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 605
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 608
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 609
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 647
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 DISULFID 122..123
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 681 AA; 72914 MW; 079F461331506962 CRC64;
MCLLTSSVLA ETTGGGAATV DGARIVAADK EPGNWLSTGR TYAEQRYSPL NAITTDNVKQ
LGLAWSYETG ANRGHHATPI VIDGIMYVTA PWSVVHALDA KTGKALWTYD PEVPKEWGKF
ACCDVVNRGV AVWEGKVIFG TLDARLVAVD AATGKKAWEV DTKEGPWPYT ITGAPRVVKG
KVIIGNGGAE YGVRGYVTAY DAATGKQVWR FYTVPGDPAK PFENPELAEA AKTWTGEWWK
MGGGGSVWDS MAFDPELNTL YVGTGNGSPW ARHIRSPGGG DNLFLSSILA IDPDTGRLKW
HYQTTPGDTW DYTATQHMIL AELTIDGKPR KVIMQAPKNG FFYVLDRETG QLISAKNYVT
VTWASGIDMA TGRPIENPDA RWADKPAVVM PSPIGGHNWQ PMAFNPETGL VYIPTQEIPG
LYAPDGKFAY NRKQWNTGTD NAPIADVDPA IVSGALIAWD PVAQKEVWRA KLWGPWNGGV
LTTAGNLVFQ GTSDGKFNAY DARTGERLWT SPTQTGVQAA PVTFTVDGEQ YVSVVVGYGG
AYALAYGRAA KTLDIPVVGR VLTYKIGGTA QLPKPDLSAA VPPPPPNTAP AEVVARGGAL
FAQYCMVCHG AGAVSGGVLP DLRHSGPVIH QAWKEIVLGG MLKDNGMVSF ADVLKDEDAD
AIHAYVISRA HEGDVPGTPA K
//
