PVADH_SPHS1
ID PVADH_SPHS1 Reviewed; 654 AA.
AC Q588Z1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Polyvinylalcohol dehydrogenase;
DE Short=PVA dehydrogenase;
DE Short=PVADH;
DE EC=1.1.2.6;
DE AltName: Full=Polyvinyl alcohol dehydrogenase (cytochrome);
DE Flags: Precursor;
GN Name=pvadh;
OS Sphingopyxis sp. (strain 113P3).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=292913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=113P3;
RX PubMed=15817792; DOI=10.1099/mic.0.27655-0;
RA Klomklang W., Tani A., Kimbara K., Mamoto R., Ueda T., Shimao M., Kawai F.;
RT "Biochemical and molecular characterization of a periplasmic hydrolase for
RT oxidized polyvinyl alcohol from Sphingomonas sp. strain 113P3.";
RL Microbiology 151:1255-1262(2005).
RN [2]
RP PROTEIN SEQUENCE OF 33-46, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=113P3;
RX PubMed=16804170; DOI=10.1099/mic.0.28848-0;
RA Hirota-Mamoto R., Nagai R., Tachibana S., Yasuda M., Tani A., Kimbara K.,
RA Kawai F.;
RT "Cloning and expression of the gene for periplasmic poly(vinyl alcohol)
RT dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type
RT quinohaemoprotein alcohol dehydrogenase.";
RL Microbiology 152:1941-1949(2006).
CC -!- FUNCTION: Catalyzes the oxidation of polyvinyl alcohol (PVA) in the
CC polyvinyl alcohol degradation pathway. {ECO:0000269|PubMed:16804170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a polyvinyl alcohol + 2n Fe(III)-[cytochrome c] = an oxidized
CC polyvinyl alcohol + 2n Fe(II)-[cytochrome c] + 2n H(+);
CC Xref=Rhea:RHEA:20157, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:12870,
CC Rhea:RHEA-COMP:12871, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16571, ChEBI:CHEBI:17246, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.1.2.6;
CC Evidence={ECO:0000269|PubMed:16804170};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:16804170};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2-7.4. {ECO:0000269|PubMed:16804170};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:16804170};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16804170}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:15817792}.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB190288; BAD95543.3; -; Genomic_DNA.
DR AlphaFoldDB; Q588Z1; -.
DR SMR; Q588Z1; -.
DR STRING; 292913.LH20_00830; -.
DR KEGG; ag:BAD95543; -.
DR BRENDA; 1.1.2.6; 8996.
DR BRENDA; 1.1.3.30; 8996.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047059; F:polyvinyl alcohol dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR Gene3D; 2.130.10.10; -; 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; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 7.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Iron; Metal-binding; Oxidoreductase;
KW Periplasm; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:16804170"
FT CHAIN 33..654
FT /note="Polyvinylalcohol dehydrogenase"
FT /id="PRO_0000419459"
FT DOMAIN 42..159
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 55
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 58
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 59
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:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 654 AA; 69486 MW; 5AC66DECB2E465E8 CRC64;
MGSHAWGGAV FSAATLIAFG SVVHASGTVA ETAPQSGHAV PADQLDGETL YKARCAACHD
NAEGRTPSRE VLSKNPASFI LASMRTGAMV PMAEGLTLEE MTAIARAVGK ADAKTDDGID
LRRIWGNSVE GTPLDAPQCS SAPTPVDLGA ANQWNGWSTE KDNGRFQRKP ALDVADIPKL
KLKWAFQYPG SKNGQATVIG DRLFTTSTSG AVYALNAKTG CVYWRHAAEG ATRTSPVIAA
LPEGAPAKTA LFFSDFTKAA VALDAETGKQ LWKTVVDDQP ALQMTGSITY WDGKIYVPIS
SGTEAFAQIP TWECCKFRGA LVALDAATGK ILWKRYTTEQ EPRPFKLNKA GRQMWGPSGG
AIWVTPTVDE ARRLIYVGTS NSYTDVPYDN SDSVMAIDAD TGAVRWTVQL LADDNYIDGC
WQKGKEHANC PNPLGPDFSI GAAPIYRKMA DGKEFLLVGQ KSGMIYALDP ANKGAKIWER
QLSLGSALGG IEFGTAADDG KVYAGVSDIA SQAKDRGKPG LWALDIRTGE VAWNFLNAPD
TKCRWNNWWC HGAFSQAISV IPGAIFAGSY DGHFRAFDTA TGKIIWDVDT GTKAVTTLSG
AKAFGGVMDG AGPTIAGGMV YVHSGYAGRS SESGGRDLRG TDGNILMAFS VDGK
