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Database: UniProt
Entry: A0A017HL94_9RHOB
LinkDB: A0A017HL94_9RHOB
Original site: A0A017HL94_9RHOB 
ID   A0A017HL94_9RHOB        Unreviewed;       884 AA.
AC   A0A017HL94;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Broad-specificity glycerol dehydrogenase, subunit SldA {ECO:0000313|EMBL:EYD75287.1};
DE            EC=1.1.99.22 {ECO:0000313|EMBL:EYD75287.1};
GN   ORFNames=Rumeso_03198 {ECO:0000313|EMBL:EYD75287.1};
OS   Rubellimicrobium mesophilum DSM 19309.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD75287.1, ECO:0000313|Proteomes:UP000019666};
RN   [1] {ECO:0000313|EMBL:EYD75287.1, ECO:0000313|Proteomes:UP000019666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD75287.1,
RC   ECO:0000313|Proteomes:UP000019666};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:EYD75287.1}.
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DR   EMBL; AOSK01000089; EYD75287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A017HL94; -.
DR   STRING; 442562.Rumeso_03198; -.
DR   PATRIC; fig|442562.3.peg.3146; -.
DR   HOGENOM; CLU_018478_1_0_5; -.
DR   Proteomes; UP000019666; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047955; F:glycerol dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   CDD; cd10280; PQQ_mGDH; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 2.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR017511; PQQ_mDH.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   NCBIfam; TIGR03074; PQQ_membr_DH; 1.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 1.
DR   Pfam; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 5.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EYD75287.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019666};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          180..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..212
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   884 AA;  94446 MW;  2474AD4EAC1E8F66 CRC64;
     MEAAMTEVRY RSVTEVRYGD RDATRPVPAP RSRHPWGRWL VQALGVILAL IGLVLAVGGA
     WLVALGGSWY YLLAGLGLIL SGALLLMLRM TGVWAYLLVY VATWAWAIWE VGGWDGWPLV
     PRVVAPTVLL ILVLLAIPVL SRSPRPFARY GSYGAAALAA LALGLAADGL LRPQPVLAQQ
     GAATPEPGPA VEPAPEATAP APTTPPAPDD ATATPPAAGT ATGAQATEAP PPPAIPVEAS
     EDWPTYGGGA DATRYSPLDR ITPDNVAQLQ QVWQFRAGDM PDQTSGADTE AAPGYAAETT
     PIKVGDHLYL CSAKNILLSL DAGTGREEWR HDPTISNDAI PYSATCRGVA YYANPQAAPG
     EPCAARIIEG TIDARLLAVD AATGQPCPDF GQGGQVSLLD GIGATVPGWY AVTSPPAIVR
     GVIVTGAQVS DNQAEDAPSG VIRGYDAVTG ELRWAWDMER PDLHGAPPEG EAYSRGTPNS
     WTTATGDEEL GYVYLPLGNS SVDYWGGNRT EAEDEYSSSV VAIDVATGRD VWHFQTVHYD
     VWDYDLGSQP SLVDFPTAEG TVPALILSSK QGEIYVLDRR TGEPIFAPEE RPAPQGGVEP
     ERLSPTQPFS TYHTLAFPPL TERQMWGMSP IDQLWCRIQF RRASYEGEYT PPTSDRHYIE
     YPSYNGGSDW GSLAVDAADG ILVANYNNMA NFNRLIPREE VPPGVVPVNV ASADSQDAPS
     DLSPMWGSPY AIDVNAGWRV RWTGMLCTEP PYGGIRAIDL GTGETLWDRP LGEARRNGPW
     GIPSMLPVTI GTPNNGGPLV TAGGLIFIAA TTDDMFRAID LRTGEVLWET PLPAGGQATP
     MTYESDGRQY VVLMAGGHHF MKTPIGDHVL AWALPQQPEG QPAP
//
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