ID N8YCS7_ACIGI Unreviewed; 807 AA.
AC N8YCS7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Quinate/shikimate dehydrogenase (Quinone) {ECO:0000313|EMBL:ENV17433.1};
GN ORFNames=F964_02147 {ECO:0000313|EMBL:ENV17433.1};
OS Acinetobacter guillouiae NIPH 991.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217656 {ECO:0000313|EMBL:ENV17433.1, ECO:0000313|Proteomes:UP000013148};
RN [1] {ECO:0000313|EMBL:ENV17433.1, ECO:0000313|Proteomes:UP000013148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 991 {ECO:0000313|EMBL:ENV17433.1,
RC ECO:0000313|Proteomes:UP000013148};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter guillouiae NIPH 991.";
RL Submitted (FEB-2013) 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}.
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:ENV17433.1}.
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DR EMBL; APPJ01000010; ENV17433.1; -; Genomic_DNA.
DR RefSeq; WP_004819920.1; NZ_KB849456.1.
DR AlphaFoldDB; N8YCS7; -.
DR PATRIC; fig|1217656.3.peg.2097; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_1_0_6; -.
DR Proteomes; UP000013148; Unassembled WGS sequence.
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; 1.
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 Pfam; PF13360; PQQ_2; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000013148};
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 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 807 AA; 88169 MW; 6A5E8FD995085FBF CRC64;
MTESTRTHTV LKIWCFILAL ALLVTGAFFT VGGVKLATLG GSWYFVISGV ITLASAIFIF
KKKVLGVWLF SLVFVGTIIW SLLDAGWEFW PLFSRLMFPA GLFAALMFTL PAIRRYQFQP
SASLPAFGLG ALTVLGMLIG LYQMFQPHPT VAASGQALPL VPVQADQQQS NWQHYGQDSG
GSRFAALDQI TRENVHQLKE AWRFRTGDFT TGSGNGAEDQ MTPLQVGNKI YLCTPHNNIF
ALEADSGKQL WKAEVNSKSD AWERCRGVAY FDSTEPLTQP TLAGATPVQA VANNTACLRR
VYTNTPDGRL IAVNADTGER CKDFGVDGTV DLLKGLGEGT TAPRFEVTSA PTIAGTVIVV
GSRIADNLAA DMPGGVIRAY DVITGQLRWA FDPRNPDPNH VLKEGETYKR SSANSWAAMS
YDPKMNTVFM PMGSSSVDVW GGNRQPLDHK YNSSVLALDA STGKEKWVYQ TVHNDLWDFD
LPMQPSLVDF PMKGGENQPA VVIGTKSGQF FVLDRLTGKP LTQVIEQPVK PADIPGEQYS
LTQPRSVEMP QIGNQTLTES DMWGATPFDQ LMCRIGFKSM RYEGLYTAPG KDKSLSFPGS
LGGMNWGSIA FDPSHQYMFV NDMRLGLWIQ LIEQTPEDLA IQANGGEKVN TGMGAVPMKG
TPYKVNKDRF WSKLNIPCQK PPYGTMTAID MKTRQIAWQV PMGTVEDTGP MGIKMGLKAP
IGMPTIGGPM ATQGGLVFFA ATQDYYLRAL DSSSGKELWK SRLPVGSQGT PISYVSPKTG
KQYVMVTAGG ARQSPDHGDY VIAYSLK
//