ID   A0A1P8WDA6_9PLAN        Unreviewed;      1135 AA.
AC   A0A1P8WDA6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Quinate/shikimate dehydrogenase (Quinone) {ECO:0000313|EMBL:APZ92024.1};
DE            EC=1.1.5.8 {ECO:0000313|EMBL:APZ92024.1};
GN   Name=quiA {ECO:0000313|EMBL:APZ92024.1};
GN   ORFNames=Fuma_01625 {ECO:0000313|EMBL:APZ92024.1};
OS   Fuerstiella marisgermanici.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Fuerstiella.
OX   NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ92024.1, ECO:0000313|Proteomes:UP000187735};
RN   [1] {ECO:0000313|EMBL:APZ92024.1, ECO:0000313|Proteomes:UP000187735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH11 {ECO:0000313|EMBL:APZ92024.1,
RC   ECO:0000313|Proteomes:UP000187735};
RX   PubMed=28066393; DOI=10.3389/fmicb.2016.02079;
RA   Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P.,
RA   Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J.,
RA   Kaster A.K., Rohde M., Wiegand S., Jogler C.;
RT   "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the
RT   Phylum Planctomycetes from the German Wadden Sea.";
RL   Front. Microbiol. 7:2079-2079(2016).
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000256|ARBA:ARBA00001931};
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008156}.
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DR   EMBL; CP017641; APZ92024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8WDA6; -.
DR   STRING; 1891926.Fuma_01625; -.
DR   KEGG; fmr:Fuma_01625; -.
DR   Proteomes; UP000187735; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0047519; F:quinate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 2.
DR   InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR013427; Haem-bd_dom_put.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   NCBIfam; TIGR02603; CxxCH_TIGR02603; 1.
DR   PANTHER; PTHR32303:SF10; OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAMB; 1.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   Pfam; PF06439; 3keto-disac_hyd; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   Pfam; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 5.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS51007; CYTC; 2.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:APZ92024.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187735};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          503..577
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          609..749
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          382..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1135 AA;  125094 MW;  6847834419DE11F5 CRC64;
     MVPRPPALLV VFQSDNSMNM TGYSLRTLAL SLVCCFVVTT ECVSADPDRL DNHVEWGIYR
     GDKKGNQFAE LAQINAANVH RLQPAWEYNT GDAGKRTSMY SNPIIVDGRL YVCTPSLNAA
     CVDAKTGEQI WFFDSSKHNN GRVLQGRNRG VVYWEGEQGK RIFVFVKNRV YAVDALTGEL
     IKDFGDDGHI DLRKNLDMDP GKASVECTCP GVIYKNMLIV ASRVPEGYIS TPGHIRAYDT
     VTGEFRWIFH TIPKPGEFGY DTWEFVEGEV YGGANAWGGF TLDEGRGWVF CATGSPSYDF
     YGGFRKGMNL FGNCVLALNA NTGERVWHYQ TVHHDLWDMD NPSAPVLVTV DEDGKKRDLV
     VQFTKMGFTF VLDRETGKPV FDTPEVKVPP STVPGEEAWP TQPIPVRPPP LNRLALTEAD
     LTRISPEAYK KAKAKFDQYA KGPLYTPPSL EGHILTPGTL GGTEWHGGAY DPFLNTIYVN
     SHEVPSFYKL REVVTSIGDK PTSPVEHGSM LYQLTCAGCH RPDRRGAMPL IRPLLNVKKT
     DAEIKETITN GQGLMPAFHV FSDRELDALT AFIRSEPDAK TEATSEKSLE QQLLEEGAQS
     LAAASLKKGD AARGAAVFHQ PQMVCSKCHI AGDKKNSLGT DLTNLPDDAT NLHLVESILE
     PSKVIRRGYE QVSLVLSSGR VRTGFIVEER DDSIVFRDSS TKDATSVIAK SDIDDRKASE
     TSIMLAGQVN QLEDRQEFLD LVRYLIEIRD GGAKRAAELQ PDAAATALKI PKTRVRYLNE
     GYQNFTGPNG EPAITPPWGT LNAIDLVKGE ILWRVPLGEY PELVAKGIRN TGSLSFGGAV
     ATAGGLIFVA GTPDEKIRAF EKHSGRLLWE YKLPVGAYAT PSTYMIDGQQ YLAIAAGGGG
     KNGTKSGDSV IAFALPDIKD AAPKQQTADA SKDGWIDLFN GQNLDGWVHL NGSHDFFVED
     GAIVGRAVQD SVESFLCTTR EFGDFELEVE IDIDDATRSG IQIRSQVRTT TVGKGWNKTA
     GRVYGPKVEL RQNAGDGTPT TGMFLGEAME AGWLSSKDTI QKGHDFLKKD GWNQVRIVAE
     GNRMRSWVNG NLVDDISRDD IYKTHPKGFI GLQLHRDKDQ GHSVTKFRKL RIKER
//