Reviewed, UniProtKB/Swiss-Prot Q59086 (QUIA_ACIAD)

Names and origin

Protein names

Recommended name:
    Quinate/shikimate dehydrogenase [Pyrroloquinoline-quinone]
    EC=1.1.99.25
Alternative name(s):
    NAD(P)-independent quinate dehydrogenase

Gene names

Name:	quiA
Ordered Locus Names:	ACIAD1716

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	809 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Can act either on quinate or on shikimate.
Catalytic activity	Quinate + pyrroloquinoline-quinone = 3-dehydroquinate + reduced pyrroloquinoline-quinone. Shikimate + pyrroloquinoline-quinone = 3-dehydroshikimate + reduced pyrroloquinoline-quinone.
Cofactor	PQQ.
Pathway	Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3-dehydroquinate from quinate (PQQ route): step 1/1.
Subcellular location	Cell membrane; Multi-pass membrane proteinPotential.
Induction	By protocatechuate.
Sequence similarities	Belongs to the bacterial PQQ dehydrogenase family.

Ontologies

Keywords
Biological process	Quinate metabolism
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Oxidoreductase
PTM	PQQ
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW quinate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro quinate dehydrogenase (pyrroloquinoline-quinone) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 809	809	Quinate/shikimate dehydrogenase [Pyrroloquinoline-quinone]		PRO_0000205340
Regions
	Transmembrane	14 – 34	21	Potential
	Transmembrane	41 – 61	21	Potential
	Transmembrane	68 – 88	21	Potential
	Transmembrane	90 – 110	21	Potential
	Transmembrane	127 – 147	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q59086-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 71F67CEBEA62BFCB	FASTA	809	88,196
	10 20 30 40 50 60 MSDPQEKSHI ILKVWCFILG LALLITGAFY VIGGGKLISL GGSWYFLIAG LMITTSAFFM 70 80 90 100 110 120 FKKKATGVWL YALAFIGTVI WALIDAGFEF WPLHSRLMFP AGLFAAVMLT LPSIRKYQYQ 130 140 150 160 170 180 TPMSAPAYVI GGLTVLGMLG GLYGMFIPHE TVKASGEELP LVPVDPAKKQ VNWDHYGNDA 190 200 210 220 230 240 GGSRFVALDQ INRNNVSKLK EAWRFRTGDF TTGTGNGAED QMTPLQVGNK VFLCTPHNNI 250 260 270 280 290 300 FAIDADSGKQ LWKAEVNSTA DAWERCRGVA YFDSTQPLVQ PTLAGATPVA ALAANTECPR 310 320 330 340 350 360 RVYTNTVDGR LIAVNADTGA RCKDFGVNGT VNLHEGLGEN TKAPRFEVTS APTIAGTTIV 370 380 390 400 410 420 VGSRIADNVA ADMPGGVIRA YDVITGKLRW AFDPRNPDPN YVLKPGEIYK RSSTNSWAAM 430 440 450 460 470 480 SYDPQMNTVF LPMGSSSVDV WGGNRTAADH KYNTSVLALD ATTGKEKWVY NTVHNDLWDF 490 500 510 520 530 540 DLPMQPSLVD FPMKDGTTKP AVVIGTKSGQ FYVLDRVTGK PLTKVIEQPI KVADIPGEQY 550 560 570 580 590 600 SKTQPRSVEM PQIGNQTLKE SDMWGATPFD QLMCRINFKS MRYDGLYTAP GTDVSLSFPG 610 620 630 640 650 660 SLGGMNWGSI AFDPTHRYMF VNDMRLGLWI QLIKQTPEDI KIQANGGEKV NTGMGAVPMK 670 680 690 700 710 720 GTPYKVNKNR FMSALGIPCQ KPPFGTMTAI DMKTRQVAWQ VPLGTIQDTG PMGIKMGLKA 730 740 750 760 770 780 PIGMPTIGGP MATQGGLVFF AATQDYYLRA FNSSNGKELW KARLPVGSQG TPMSYMSPKT 790 800 GKQYVVVSAG GARQSPDHGD YVIAYALEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains quiA, the structural gene for quinate-shikimate dehydrogenase." Elsemore D.A., Ornston L.N. J. Bacteriol. 176:7659-7666(1994) [PubMed: 8002591] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus." Elsemore D.A., Ornston L.N. J. Bacteriol. 177:5971-5978(1995) [PubMed: 7592351] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L05770 Genomic DNA. Translation: AAC37161.1. CR543861 Genomic DNA. Translation: CAG68558.1. Different initiation.
PIR	A55547.
RefSeq	YP_046380.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2879574.
GenomeReviews	Gene locus ACIAD1716 in contig CR543861_GR.
KEGG	aci:ACIAD1716.
NMPDR	fig|62977.3.peg.1642.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q59086.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD1716-MON. MetaCyc:MON-28.
Family and domain databases
InterPro	IPR017511. PQQ_mem_DH. IPR002372. PQQ_repeat. IPR011047. Quino_AlcDHase-like. IPR001479. Quinoprotein_DHase_PQQ_bac_CS. [Graphical view]
Gene3D	G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 1 hit.
Pfam	PF01011. PQQ. 6 hits. [Graphical view]
SMART	SM00564. PQQ. 7 hits. [Graphical view]
PROSITE	PS00363. BACTERIAL_PQQ_1. 1 hit. PS00364. BACTERIAL_PQQ_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

QUIA_ACIAD

Accession

Primary (citable) accession number: Q59086
Secondary accession number(s): Q6FBK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)