ID A0A2Z5FWN7_9BACT Unreviewed; 735 AA.
AC A0A2Z5FWN7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Glucose dehydrogenase, PQQ-dependent {ECO:0000313|EMBL:AXC10927.1};
GN ORFNames=ACPOL_1581 {ECO:0000313|EMBL:AXC10927.1};
OS Acidisarcina polymorpha.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidisarcina.
OX NCBI_TaxID=2211140 {ECO:0000313|EMBL:AXC10927.1, ECO:0000313|Proteomes:UP000253606};
RN [1] {ECO:0000313|EMBL:AXC10927.1, ECO:0000313|Proteomes:UP000253606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBC82 {ECO:0000313|EMBL:AXC10927.1,
RC ECO:0000313|Proteomes:UP000253606};
RX PubMed=30510549; DOI=10.3389/fmicb.2018.02775;
RA Belova S.E., Ravin N.V., Pankratov T.A., Rakitin A.L., Ivanova A.A.,
RA Beletsky A.V., Mardanov A.V., Sinninghe Damste J.S., Dedysh S.N.;
RT "Hydrolytic Capabilities as a Key to Environmental Success: Chitinolytic
RT and Cellulolytic Acidobacteria From Acidic Sub-arctic Soils and Boreal
RT Peatlands.";
RL Front. Microbiol. 9:2775-2775(2018).
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; CP030840; AXC10927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5FWN7; -.
DR KEGG; abas:ACPOL_1581; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000253606; 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.
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:UP000253606};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 487..563
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 735 AA; 80079 MW; 060B92374D74E353 CRC64;
MGHANDRVST RRLLCTNLKG RKVRRIAVTA IVLLSSLVIR STRASDKVEA PEDWATYGGN
SSGNHYSPLN KVNRENVQHL REVWRVDVGK GGGLQTNPLV VGRRMFVYTP SEDILALDAA
TGKQLWRFSA GVPAPQPNRG FSYWRDGRES ILFAGIMDHL YALDPATGHP LKAFGEDGKI
DLRKDLGDQD YTQNFAVLTT PGTIYKDMII VGFRAPETQP APHGDIRAYD VHTGKLRWSF
HTIPHPGDPG YESWPKDAWR VTGSANNWSG MVVDLQRGIL FAPTGSAVND FYGADRVGDD
LYSDTLLALD ANTGKEIWHF QAVHHDIWDR DFPSPPVLVT VKRDGKPVDA VAQTTKQGFV
FLFERTTGKP LFPIEEKSYP ASDVPGEVTA PTQPLPVTPA PFARQRLTAD MLTNRTPAAH
TWAEEQFKTF RSEGQFVPFT VGRPTIIFPG YDGGAEWGGA AVEPTRAILY VNANDIPWTG
ELAPTQAAAS EGATIYQSQC AVCHGHDRKG SPPEFPSLLE VKKRLSDAAI SDIIHNGRGR
MPSFPALQDG GLEAVLKYLG ESPGMADLAK VDPQAPSSKT EVGSEASGSK QLPKYQFTGY
KKFYDPDGYP AVVPPWGTLN AIDLNTGSYR WKVPLGNYPE LAAAGMKATG SENYGGPVIT
GGGLLFIAAT IYDRKIRAFN SDTGELLWEG SLPFAGTATP ATYMIDGNQY IVIATSGQRD
KKGPQGAAYI VFALP
//
