ID A0A3G2L571_9FLAO Unreviewed; 712 AA.
AC A0A3G2L571;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Pyrroloquinoline quinone-dependent dehydrogenase {ECO:0000313|EMBL:AYN67393.1};
GN ORFNames=D1013_08450 {ECO:0000313|EMBL:AYN67393.1};
OS Euzebyella marina.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Euzebyella.
OX NCBI_TaxID=1761453 {ECO:0000313|EMBL:AYN67393.1, ECO:0000313|Proteomes:UP000276309};
RN [1] {ECO:0000313|EMBL:AYN67393.1, ECO:0000313|Proteomes:UP000276309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN62 {ECO:0000313|EMBL:AYN67393.1,
RC ECO:0000313|Proteomes:UP000276309};
RA Xue C.;
RT "The reduced genetic potential of extracellular carbohydrate catabolism in
RT Euzebyella marina RN62, a Flavobacteriia bacterium isolated from the hadal
RT water.";
RL Submitted (AUG-2018) 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}.
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DR EMBL; CP032050; AYN67393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G2L571; -.
DR KEGG; emar:D1013_08450; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000276309; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR CDD; cd10280; PQQ_mGDH; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
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 PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 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; 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 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}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000276309};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 479..556
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 712 AA; 77628 MW; 571CF620DB307AB6 CRC64;
MGHSKIYLTI LTLTTVFFLS CNSNQTSNSK EQWFTHRGDL ESSNYSGAEQ IKVDNVKDIE
LAWSFNMNDM PDGSRAGLSQ CTPIVVKGVM YTMSAKAILY ALDAATGKQI WQFDPFNGQQ
GGGTVRGVAY WEKNGDSRIL FGAGPTLIAV NAEDGKPITD FGKNGAVDLR IGLRDDPSDL
FTALTSPGVI YEDLYIVGGR LEDLYGSPPG YIRAYNVITG ELTWTFHTIP KPGEPGYETW
PKEAYKTAGG ANNWAGMSVD TKRGLVFASL GSPSYDFYGA DRLGQNLYGN CVLALDAATG
DYVWHYQTVH HDLWDYDLPA PPNLVTLKKD GIDIDAVAQI TKQGFVFVLD RDTGEPIFPI
EEKSVPESFM PGEKAWPTQP FPTRPLPFAR QYMTVEDLND VSAENNLALQ KQFDSLRYEG
MYTPPDLKGT VMIPGTRGGA QWGGAAFDKE TNTLYIRSMD VAELITIVER DPAKIKATST
IEQGGNLYKN YCAACHGANR QGNGAVFPEL TNVKSRLSKE IAKTKITGGV GQMPGFSRAL
TDDEIESLLA FLYEEEDRVI SEEAASTSQN DKIEYYNISG YTTWIDQSGN PAIKPPWGTL
HSLDLSSGEY NWQVPLGNNP ELQKDGAPLT GLEGKSGPIV TAGGLIFIGG AEDKLLRAID
KSNGQTLWEY ELPAMANATA CTYEVGGKQY VSISVGGTTE NPSGSVMAFA LK
//