ID Q4JIU2_9BACT Unreviewed; 609 AA.
AC Q4JIU2;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=XoxF {ECO:0000313|EMBL:AAY96669.1};
OS uncultured bacterium BAC10-4.
OC Bacteria; environmental samples.
OX NCBI_TaxID=333425 {ECO:0000313|EMBL:AAY96669.1};
RN [1] {ECO:0000313|EMBL:AAY96669.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16332881; DOI=10.1128/AEM.71.12.8846-8854.2005;
RA Kalyuzhnaya M.G., Bowerman S., Nercessian O., Lidstrom M.E.,
RA Chistoserdova L.;
RT "Highly divergent genes for methanopterin-linked C1 transfer reactions in
RT Lake Washington, assessed via metagenomic analysis and mRNA detection.";
RL Appl. Environ. Microbiol. 71:8846-8854(2005).
RN [2] {ECO:0000313|EMBL:AAY96669.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16109948; DOI=10.1128/JB.187.17.6069-6074.2005;
RA Vorholt J.A., Kalyuzhnaya M.G., Hagemeier C.H., Lidstrom M.E.,
RA Chistoserdova L.;
RT "MtdC, a novel class of methylene tetrahydromethanopterin dehydrogenases.";
RL J. Bacteriol. 187:6069-6074(2005).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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; DQ084247; AAY96669.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4JIU2; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR001479; Quinoprotein_DH_CS.
DR NCBIfam; TIGR03075; PQQ_enz_alc_DH; 1.
DR PANTHER; PTHR32303:SF22; METHANOL DEHYDROGENASE LARGE SUBUNIT-LIKE PROTEIN; 1.
DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW PQQ {ECO:0000256|ARBA:ARBA00022891}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..609
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004239098"
SQ SEQUENCE 609 AA; 65587 MW; 1F157FD7AF6A748A CRC64;
MKCRNWVALV AAFSFSGGAF ANDELLGLQK DDKQWVMAGK NYSANRYSTL AQVTTANVKQ
LKEAWSFSLG ALRGHEGAPL VVGSTMYAHS SFSDSESSPG PHIYALDLTK EGAPIKWTYT
PKTDKRAVPV ACCDVVQRGL NYAAGKILFN TLDGQVIALD AGTGKEVWKI KNANPQNGET
MTMAGLVVKN NFIVGVSGGE FGIRGWVAAY NINDGKQAWK AYSMGPDEDV KLAADFNSAN
PQHGQKGLGT STWPGEQWKI GGGSTWGWYS YDPELNLFYY STGNPGTWNP TPRKGDNKWS
MTIFARNPDT GEAKWAYQMT PWDAWDYDGV NEHQLADLTI GGKPVKALVH FDRNGFGYTL
DRTNGTLLVA KPFVYVNWAT GIDLKTGRPI EDPANARSRA RTPRTSALAP WVARTSSPSA
YSPKTGLFYV PTNNMCMNYE GVEVKYQSGA PYVGANVLMM PGRADMTGAP SDGHVGDFIA
WDATTGKRVW TLKEAQPVWS GALATAGGVV FYATLDGWFK AVDDKTGALL WKHKLAAGSI
GNPMTYVGPD GKQYVAIYSG PGGWYAAPVA ANLSKDDPFG ALGAVGVAFG ANLDKATSVG
GTLHVFSIQ
//
