ID I2QBF4_9BRAD Unreviewed; 618 AA.
AC I2QBF4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:EIG57110.1};
GN ORFNames=Bra1253DRAFT_01765 {ECO:0000313|EMBL:EIG57110.1};
OS Bradyrhizobium sp. WSM1253.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319003 {ECO:0000313|EMBL:EIG57110.1, ECO:0000313|Proteomes:UP000005125};
RN [1] {ECO:0000313|EMBL:EIG57110.1, ECO:0000313|Proteomes:UP000005125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1253 {ECO:0000313|EMBL:EIG57110.1,
RC ECO:0000313|Proteomes:UP000005125};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "Improved High-Quality Draft sequence of Bradyrhizobium sp. WSM1253.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1253 {ECO:0000313|Proteomes:UP000005125};
RX PubMed=26629308;
RA Tiwari R., Howieson J., Yates R., Tian R., Held B., Tapia R., Han C.,
RA Seshadri R., Reddy T.B., Huntemann M., Pati A., Woyke T., Markowitz V.,
RA Ivanova N., Kyrpides N., Reeve W.;
RT "Genome sequence of Bradyrhizobium sp. WSM1253; a microsymbiont of
RT Ornithopus compressus from the Greek Island of Sifnos.";
RL Stand. Genomic Sci. 10:113-113(2015).
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; JH600073; EIG57110.1; -; Genomic_DNA.
DR RefSeq; WP_007592931.1; NZ_JH600073.1.
DR AlphaFoldDB; I2QBF4; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_0_0_5; -.
DR Proteomes; UP000005125; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 CDD; cd10278; PQQ_MDH; 1.
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 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; 5.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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 PQQ {ECO:0000256|PIRSR:PIRSR617512-2}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..618
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003663963"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 87
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 144
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 188
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 270
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT DISULFID 138..139
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 618 AA; 67110 MW; E7B6F8E24E7C0CE1 CRC64;
MLVRGLTRLL GLLPGILCAL CASCAVLSSA SAQSDLANRM KDPAQWPMAA RDYANTRYSE
LDQINASNAS RLQLAWTFSV GADRGQEAAP LVVDGTMYVV GPYAGPYPNR VFALDATTGE
LKWSYAPKPE PAAAGVACCD VVNRGLAFDN GKIFLNTLDN HTVAIDAKSG KELWHTKLGE
INKGETITMA PVVVRGKILV GNSGGEMGVR GWVTALDETT GAITWRAYST GPDKDVLIGD
DFKPYYDSLK GKDLGVKTWP ADRWQIGGGT VWGWISYDPE LNLIYYGTAN PSPWNANQRS
GDNLWSTTIF ARDPDTGRAK WAYQINPHDL FDHDEINENV LVDLELNGKP RKVLIHPGRN
GYMYVMDRAT GEVISADAYD FVNSYKGVDL KTGKIIPNEE KMPLVGKTVE NICPSAPGAK
DWQPTAWSPR TKLLYVPHQH LCMSFKASQV GYIAGTPYVG ADVDMYAGPG GYRGEFMAWD
PIARKKVWEI HEKLPVWSGA LVTAGDVAFY GTMDRLFKAV DAKDGHVLWQ FRAGSGFIGQ
PISYRGSDGQ QYVAILSGVG GWPGVVANAE VDQRVRNAAL GFTGATQDLP FYTAGGSELL
VFKLGGAFGE DTSHAPSK
//
