ID F7S965_9PROT Unreviewed; 615 AA.
AC F7S965;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Pyrrolo-quinoline quinone {ECO:0000313|EMBL:EGO94298.1};
GN ORFNames=APM_2882 {ECO:0000313|EMBL:EGO94298.1};
OS Acidiphilium sp. PM.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=1043206 {ECO:0000313|EMBL:EGO94298.1, ECO:0000313|Proteomes:UP000004823};
RN [1] {ECO:0000313|EMBL:EGO94298.1, ECO:0000313|Proteomes:UP000004823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM {ECO:0000313|EMBL:EGO94298.1,
RC ECO:0000313|Proteomes:UP000004823};
RX PubMed=21914891; DOI=10.1128/JB.05386-11;
RA San Martin-Uriz P., Gomez M.J., Arcas A., Bargiela R., Amils R.;
RT "Draft Genome Sequence of the Electricigen Acidiphilium sp. Strain PM (DSM
RT 24941).";
RL J. Bacteriol. 193:5585-5586(2011).
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:EGO94298.1}.
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DR EMBL; AFPR01000462; EGO94298.1; -; Genomic_DNA.
DR RefSeq; WP_007424019.1; NZ_AFPR01000462.1.
DR AlphaFoldDB; F7S965; -.
DR HOGENOM; CLU_018478_0_0_5; -.
DR Proteomes; UP000004823; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 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; 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, ECO:0000256|PIRSR:PIRSR617512-3};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR617512-4};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR617512-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW PQQ {ECO:0000256|ARBA:ARBA00022891, ECO:0000256|PIRSR:PIRSR617512-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..615
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003362196"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 93
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 147
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 191
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 275
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT DISULFID 141..142
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 615 AA; 66918 MW; F88760BE98D7C6ED CRC64;
MTRLGTKSLK RSLLAASFGI LGAGALVLSA QAATSGSANE SLLQMQKNPN DWVMPTGTYN
NWRYSTLDQI NSKNVKNLQV AWTMSTGTDR GLEGQPIVIG DMMYYETSYP NYVYAVNLNH
PDQIAWKYTP PRDSNAPPVA CCDVVNRGPA YGDGMIFVDA LDARLYALNA KTGKVVWSAD
NGHPKDGQTM TGAPMVVGNN VIVGIAGGEY GVRGYITAYN IHTGKMVWRG YSEGPSKDTL
IDPATTINGA TGKPVGPHSS IKTWKGDEWK VGGGTTWGWY SYDPKLNLIY YGSGNPGTWN
PSQRPGKNRW SMTIWARNPE TGKVKWVYQM TPHDGWDYDG VNEMVLVNVK YHGKEVPALV
HFDRNGFSYV MNRENGSPIA IHKYDPSVNW ATGINPKTNE PIVDPAKMTE AGKDVKDICP
SSQGDKDEQP VSYDPKTGLF YAPLNHLCMS YQAFNVKYKA GFPFVGAIVN MIPGPGGYRG
RFIAYNPMTG KTEWQIHDMF QDWGGALTTA GNVAFYGTLK GMFRAVDIKT GKILYQFKTP
SGIIGNPITY MHDGKQYVAV LSGVGGWAAI GMADNLHKSS AGLGAVGLNA TLTDYTNLGG
TLMVFSLPSK VASAN
//
