ID A0A2S8B1M0_9SPHN Unreviewed; 728 AA.
AC A0A2S8B1M0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:PQM26226.1};
GN ORFNames=CVO77_14245 {ECO:0000313|EMBL:PQM26226.1};
OS Sphingopyxis lindanitolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=2054227 {ECO:0000313|EMBL:PQM26226.1, ECO:0000313|Proteomes:UP000238954};
RN [1] {ECO:0000313|Proteomes:UP000238954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS5A3p {ECO:0000313|Proteomes:UP000238954};
RA Kaminski M.A.;
RT "The complete genome sequence of Sphingopyxis pomeranensis sp. nov. strain
RT WS5A3p.";
RL Submitted (NOV-2017) 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:PQM26226.1}.
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DR EMBL; PHFW01000003; PQM26226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8B1M0; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000238954; Chromosome.
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; 6.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 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:UP000238954};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..728
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015609898"
FT DOMAIN 633..712
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 96
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 148
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 192
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 208..209
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 272
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 364
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 427..428
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 646
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 649
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 /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 689
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 142..143
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 728 AA; 77720 MW; 157C83D9A61E9963 CRC64;
MAKKVFSAAL LGCAALALAA CNASKNDSIS GGGSLDDAEK ASEALLKTGG NGDDWAGIGY
SYDEQRFSPL TDINDKNVGG LGIAWYADLD DARGQEATPV VVDGVMFVSH AWSKVDAWDA
ATGKKLWSFD PKVPGERAVS ACCDVVNRGV AVWGDKLFVG TLDGRLIALD RKTGKELWST
QTFDTSKPYT ITGAPRVVKD MVLIGNGGAE FGVRGYVTAY DADTGKERWR FYTAPNPEKK
KDGAASDDIF AAKGNATWSD KGEWKVSGGG GTVWDAIVYD KDLDQIYLGV GNGNPWNHGE
RSNGEGDNWF LSSVVALDAD TGAYKWHYQE TPAESWDYTA TQPIILAEQA VNGKPTKVLY
HAPKNGFFFT IDRTNGKLID AKPYVDGINW ATGYDMATGR PIENPDARFY RTGKPFIAIP
GALGAHNWHP MSYNPATGLV YIPAQQIPQG YLQDMDELDK RKVLGFNVGT SLNKTMLPDD
KAAFRAAVAA TTGRLVAFDP RTGKVAWGVD YPAAWNGGTM TSAGNLVFQG TSTGRFRAYA
ADTGKQLLDL DMQSGIVSAP STFRVGGVQY VAFQTGKGGA FPLVAGVAGG VTRKLPNLPR
LVVLKVGGTV KLPAPPATTT LAWNPPPQFG TPQQVAAGKA HFGRYCIVCH GDSAIGNGFT
PDLRVSGALT NADAWKSVIL DGALKDRGMV SFARVLTPAD VEAIRAYVID RSHWTKANLP
EATAPVGR
//