ID   PVADH_PSESP             Reviewed;         639 AA.
AC   P77931;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=pvaA;
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=VM15C;
RX   PubMed=8782398; DOI=10.1271/bbb.60.1056;
RA   Shimao M., Tamogami T., Nishi K., Harayama S.;
RT   "Cloning and characterization of the gene encoding pyrroloquinoline
RT   quinone-dependent poly(vinyl alcohol) dehydrogenase of Pseudomonas sp.
RT   strain VM15C.";
RL   Biosci. Biotechnol. Biochem. 60:1056-1062(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VM15C;
RX   PubMed=10746768; DOI=10.1099/00221287-146-3-649;
RA   Shimao M., Tamogami T., Kishida S., Harayama S.;
RT   "The gene pvaB encodes oxidized polyvinyl alcohol hydrolase of Pseudomonas
RT   sp. strain VM15C and forms an operon with the polyvinyl alcohol
RT   dehydrogenase gene pvaA.";
RL   Microbiology 146:649-657(2000).
CC   -!- FUNCTION: Catalyzes the oxidation of polyvinyl alcohol (PVA) in the
CC       polyvinyl alcohol degradation pathway. {ECO:0000269|PubMed:8782398}.
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; Evidence={ECO:0000269|PubMed:8782398};
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000269|PubMed:8782398};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8782398}.
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; D50670; BAA09321.1; -; Genomic_DNA.
DR   EMBL; AB008494; BAA94193.1; -; Genomic_DNA.
DR   PIR; JC4881; JC4881.
DR   AlphaFoldDB; P77931; -.
DR   SMR; P77931; -.
DR   BRENDA; 1.1.2.6; 5085.
DR   GO; GO:0005737; C:cytoplasm; 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   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   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 7.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   SUPFAM; SSF50998; SSF50998; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Heme; Iron; Metal-binding; Oxidoreductase; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..639
FT                   /note="Polyvinylalcohol dehydrogenase"
FT                   /id="PRO_5000139986"
FT   DOMAIN          36..152
FT                   /note="Cytochrome c"
FT   BINDING         49
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   639 AA;  68049 MW;  406E9EF873963B8A CRC64;
     MQQNIERNQV SMTTSRFVWG AVMALVALGS ASAAELNLPD GAALYRARCG TCHDNPQDRT
     PARDVIARNS PAFIMAAMNG VMAPMAAGLS EAEKQAIALH LGARPAGGSQ EINPHAIWGP
     PSASMPLDGP KCKGKIPPID LSTPDQWNGW GAGITNARFQ PNPGLTAADV PRLKVKWAFN
     YPGSKNGQAT VVGDRLFVTS MSGAVYALNA KTGCVYWRHD AAAATRSSVH VVQLPAGAPA
     QYAIFFSDWT KAAVALDAQT GKQLWKTTID DQPGVQMTGS PTYHEGKLFV PISSGNEAFA
     TNDQWECCKF RGALVALDAL SGKVLWKTYT TQKEPAPFRL NKLGKQMWGP AGGSIWSAPT
     IDPKRGLVYV ATSNSYTEVH HEGSDAVMAM EIETGKVRWI NQVTKDDNYI IGCPRAANCP
     EKVGPDFALG NSPILHTLQD GRQYIVVGQK SGAVYAMDPD NDGELIWMRR VSPGSELGGV
     EFGMAADAEN VYVGISDVIT RKGGKPGVYA LRIRDGADVW AFPAPRTPCR WNNIFCHPAV
     SQAVTAMPGV VFAGSMDGHF RAFSTSDGKV LWEFNTAAAP YKTVAGKQAD GGVMDGAGPT
     IAGGMVYVHS GYAGRSTQNA GDLRGREGNV LIAFSVDGK