ID A0A077F999_9PSED Unreviewed; 805 AA.
AC A0A077F999;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Quinate/shikimate dehydrogenase {ECO:0000313|EMBL:AIL61035.1};
GN ORFNames=PSAKL28_18110 {ECO:0000313|EMBL:AIL61035.1};
OS Pseudomonas alkylphenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL61035.1, ECO:0000313|Proteomes:UP000028931};
RN [1] {ECO:0000313|EMBL:AIL61035.1, ECO:0000313|Proteomes:UP000028931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KL28 {ECO:0000313|EMBL:AIL61035.1,
RC ECO:0000313|Proteomes:UP000028931};
RA Lee K., Lim J.Y., Hwang I.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000256|ARBA:ARBA00001931};
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008156}.
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DR EMBL; CP009048; AIL61035.1; -; Genomic_DNA.
DR RefSeq; WP_038609287.1; NZ_CP009048.1.
DR AlphaFoldDB; A0A077F999; -.
DR KEGG; palk:PSAKL28_18110; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_1_0_6; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000028931; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR CDD; cd10280; PQQ_mGDH; 1.
DR Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 2.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017511; PQQ_mDH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR001479; Quinoprotein_DH_CS.
DR NCBIfam; TIGR03074; PQQ_membr_DH; 1.
DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 1.
DR Pfam; PF01011; PQQ; 2.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW PQQ {ECO:0000256|ARBA:ARBA00022891};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 805 AA; 84950 MW; F0665CC30FEA5F1F CRC64;
MKHAPRTSGA SIFILVGLGV IIALLGLALA AGGVKLVSLG GSWYFLIGGL LMAVSGLLVA
RRKPAGAWLY AAFLVGTAIW ALADVGLVFW PLFSRLFMFG AIGLALALVY PMLARAAGNT
PGRSAYGVAG VLAVALVIAA GNMFVAHPSV APTGNGPGVT AVDPANAQKD WAHYGNTEGG
SRFAALDQIN RNNVNQLKVA WTYHTGDVAF SDGNGAEDQL TPLQIGNKVF ICTPHNNLIA
LDADTGKELW KNAINAKSAV WQRCRGMAYF DATAPIAQPT QATASAIIAA SVPAGANCQR
RLLTNTIDAR LIAVDADTGE FCQGFGNNGQ VDLKTGLGNV PDSYYQLSSA PLMAGTTVVV
GGRIADNVQT DMPGGVIRGF DVISGQMRWA FDPGNPEDRN APSGDSTYVR STPNSWAPMS
YDPAMNTLFL PMGSSSTVIY GVERTELNHK YGASVLALDA SSGEEKWVYQ TVHNDLWDFD
LPMQPSLIDF TKADGLSVPA LVIGTKAGQI FVLDRATGKP LTQVEEVAVK AGNIPNEPYS
PTQPKSVGMP QIGAQQLTES DMWGATPYDQ LLCRIDFKKM RYDGLYTAPG TDLSLSFPGS
LGGMNWGSIS TDPVHGFIFV NDMRLGLWIQ MIPSQNSGQA SSGGEALNTG MGAVPLKGTP
YAVNKNRFLS VAGIPCQAPP FGTLTAIDMK TQKVAWQVPV GTVEDTGPLG IRMHLPIKVG
LPTLGGTLST QGGLVFIAGT QDFYLRAFNS GNGEEVWKAR LPVGSQGGPM TYVSPKTGKQ
YIVITAGGAR QSTDRGDYVM AYALP
//