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Database: UniProt
Entry: A0A2U1VLX4_9PROT
LinkDB: A0A2U1VLX4_9PROT
Original site: A0A2U1VLX4_9PROT 
ID   A0A2U1VLX4_9PROT        Unreviewed;       579 AA.
AC   A0A2U1VLX4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:PWC35561.1};
GN   ORFNames=TSO221_29285 {ECO:0000313|EMBL:PWC35561.1};
OS   Azospirillum sp. TSO22-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=716789 {ECO:0000313|EMBL:PWC35561.1, ECO:0000313|Proteomes:UP000245126};
RN   [1] {ECO:0000313|EMBL:PWC35561.1, ECO:0000313|Proteomes:UP000245126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSO22-1 {ECO:0000313|EMBL:PWC35561.1,
RC   ECO:0000313|Proteomes:UP000245126};
RA   Jang J., Ishii S.;
RT   "Comparative genome analysis of Azospirillum sp. strains.";
RL   Submitted (JUL-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWC35561.1}.
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DR   EMBL; LGQZ01000141; PWC35561.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1VLX4; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000245126; 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; cd10277; PQQ_ADH_I; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR   InterPro; IPR034119; ADHI.
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; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   PANTHER; PTHR32303:SF20; QUINOPROTEIN ETHANOL DEHYDROGENASE; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 6.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245126};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..579
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015470151"
FT   ACT_SITE        315
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         84
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         134
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         178
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         196
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         273
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         315
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         410..411
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   DISULFID        128..129
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   579 AA;  62680 MW;  D55F91D1E1864537 CRC64;
     MKRLISTFAL AAGLAVWAAA AVAGPVSNDD ILKDATSTGD VLSYGLGPQG QRFSPLAKLT
     PETVAKLVPA WSFSFGGEKQ RGQEAQPLVH DGVMYVTGSY SRLFAVDART GQKKWQYDHR
     LPEGIMPCCD VVNRGAAIHG NKVYFTTLDA RLVALDKDTG KVVWNKKLAD YQAGYSNTAA
     PLVVEGKVIT GNSGGEFGIV GMVEARDAET GELVWQRPMV EGHMGTLNGK ESTMTGKLNA
     SWPGDLWKTG GGATWLGGTY DPETRTLFFG TGNPAPWNSH LRPGDNLYTS STVALNPDTG
     EIKWHYQTTP HDGWDFDGVN EFVSFDLKKD GQTIKAGAKA DRNGFFYVID RTNGKLLNAA
     PFVSKITWAK EIDLKTGRPV YIDDNRPADP SGAEKGKPVF AAPAFLGAKN WMPMAYSPQT
     ELFYVPANEW GMDIWNEPIT YKKGAAYLGA GFTIKPLYND YIGALRAMDP KTGKIVWEYK
     NPAPLWGGVL TTAGNLVFTG TPEGFLKAFD AKTGKEVWKF QTGSGVVGCP ITWEMDGEQY
     VAVASGWGGA VPLWGGDVAK LVKDINQGGS LWVFKLPKA
//
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