ID A5FZB3_ACICJ Unreviewed; 570 AA.
AC A5FZB3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Pyrrolo-quinoline quinone {ECO:0000313|EMBL:ABQ30945.1};
GN OrderedLocusNames=Acry_1741 {ECO:0000313|EMBL:ABQ30945.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30945.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ30945.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30945.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ30945.1; -; Genomic_DNA.
DR RefSeq; WP_011942456.1; NC_009484.1.
DR AlphaFoldDB; A5FZB3; -.
DR STRING; 349163.Acry_1741; -.
DR KEGG; acr:Acry_1741; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_0_0_5; -.
DR Proteomes; UP000000245; Chromosome.
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; 7.
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:UP000000245};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..570
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002683131"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 91
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 143
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 399..400
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 542
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT DISULFID 137..138
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 570 AA; 61275 MW; 29EF50F2D5C4DF79 CRC64;
MKSRFARTGT ALIGALAGTL LAAGAASAQP AYPSVTQARL DNAAASKGWL MFNRSYAGDD
YAPFAQINTK NVASLKPAWS SAKIDIPNGF EGTPIVNGDY MFATTPLDHL IAFNAKTGQK
LWEYDYDLPK TALKTVCCDV NNRGVAVYGN EVFMGTLDNH VLALDATTGK VLWNVALEKP
GIGYSISEAP MIVDGKVIIG SGGGEYGARG FIVGLDAQTG KLLWKTYTIP SPSEPGGKTW
PAGAYKHGGG SPWMTGTYDP KTKQLFWGVG NPGPWLASMR PGNNLYSDSV IAIDPNTGAI
KWHYQYTRND TWDYDGVNTA QLADITYKGK PYHALVEANR NGYFYAINRE TGKLIYAVPF
VHDTSIIGIK DGQAVNNMKL RPALDKQIFT CPSFLGGKNW WPGAVDPATN MAYVPTLHAC
MTMKGVPVSY AAGLPYLGET FEMKPDPASP HHMGSIQAID LSTGKQVWQH RTKEPWDGGA
MATSGGLVFS GTADGHLYAF DAKTGKILWK SPYLGSGIIA NPMSYEIDGK QYVAVWSGWG
GVWPLWSGKL GASLAKAPRG GQLHVFALNG
//
