ID A0A1R4H903_9GAMM Unreviewed; 566 AA.
AC A0A1R4H903;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative dehydrogenase XoxF {ECO:0000313|EMBL:SJM92676.1};
DE EC=1.1.99.- {ECO:0000313|EMBL:SJM92676.1};
GN Name=xoxF {ECO:0000313|EMBL:SJM92676.1};
GN ORFNames=CRENPOLYSF1_320005 {ECO:0000313|EMBL:SJM92676.1};
OS Crenothrix polyspora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=360316 {ECO:0000313|EMBL:SJM92676.1, ECO:0000313|Proteomes:UP000195667};
RN [1] {ECO:0000313|EMBL:SJM92676.1, ECO:0000313|Proteomes:UP000195667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSM_CP1 {ECO:0000313|EMBL:SJM92676.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR617512-3};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR617512-3};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000256|PIRSR:PIRSR617512-2};
CC Note=Binds 1 PQQ group per subunit. {ECO:0000256|PIRSR:PIRSR617512-2};
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008156}.
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DR EMBL; FUKI01000107; SJM92676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4H903; -.
DR Proteomes; UP000195667; Unassembled WGS sequence.
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; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 6.
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, ECO:0000256|PIRSR:PIRSR617512-3};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR617512-4};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR617512-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SJM92676.1};
KW PQQ {ECO:0000256|ARBA:ARBA00022891, ECO:0000256|PIRSR:PIRSR617512-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000195667}.
FT ACT_SITE 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 5
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 59
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 103
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 189
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT DISULFID 53..54
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 566 AA; 61145 MW; 103C143997DB6D0D CRC64;
MRGHEGGPLA IDGVIYIHTP FPNTVFAIDQ KTQAILWEFT PVQDADVTIP VMCCDTVNRG
LAYGDGKIFL QQSNTVLTAL DAKTGKRVWS VQNGDPKLGM TNTNAPLVVK DNVLTGISGG
EFGVRGFMAA YNMKTGKLAW KGYSMGPDSD TLIDPAKTTT WEDGKVTPVG ENSSLKTWKG
DQWKIGGGTT WGWYSYDPKL NLVYYGSGNP STWNPTQRPG DNKWSMSLWA RDADTGAVKW
VYQMTPHDEW DFDGINEVPL IDQEVNGKMH KTIVHFDRNG FGYTLDRETG ELLIAEKFDK
SVNWASHVDM KSGRPQVVSK YSTEQNGEDV KSEDICPAAL GSKNQQPVSY SPQTGLVYIS
GNHLCMNYEP FAVDYTAGQP YVGATLDMMP AGKDVLTGAP DGTSNLGQFT AWDSKTGKIA
WSVKEPFSVW SGSVATAGGV VFYGTLEGYL KAVDAKTGKE LYKFKTPSGI IGNVNTWSFE
GHQYVGVLSG IGGWAGAVVA TDGDKVIAAM QEKIAGETDP AKKAELEKAL LMKTQEALGA
AGAYASLGKL TKAGGVFSVF ALPSNK
//
