P28036 (DHET_ACEPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alcohol dehydrogenase [cytochrome c]
EC=1.1.2.8

Gene names

Name:

adhA

Organism

Acetobacter polyoxogenes

Taxonomic identifier

439 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the oxidation of primary alcohols except for methanol that is not a substrate. Ref.1
Catalytic activity	A primary alcohol + 2 cytochrome c = an aldehyde + 2 reduced cytochrome c.
Cofactor	Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-143-Cys-144 and the indole ring of Trp-280 By similarity. Binds 1 calcium ion per subunit By similarity. Binds 1 heme group per subunit By similarity.
Subunit structure	Heterotetramer (dehydrogenase, cytochrome, and two smaller unknown subunits) that forms the alcohol dehydrogenase complex.
Subcellular location	Cell membrane; Peripheral membrane protein; Periplasmic side Potential.
Sequence similarities	Belongs to the bacterial PQQ dehydrogenase family. Contains 1 cytochrome c domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding PQQ
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on CH-OH group of donors Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Chain	36 – 738	703	Alcohol dehydrogenase [cytochrome c]		PRO_0000025561
Regions
	Domain	634 – 738	105	Cytochrome c
Sites
	Active site	343	1	Proton acceptor Potential
	Metal binding	217	1	Calcium By similarity
	Metal binding	298	1	Calcium By similarity
	Metal binding	654	1	Iron (heme axial ligand) By similarity
	Binding site	650	1	Heme (covalent) By similarity
	Binding site	653	1	Heme (covalent) By similarity
Amino acid modifications
	Disulfide bond	143 ↔ 144		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P28036 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 1E2B6ED7BCD92AF6	FASTA	738	80,841
	10 20 30 40 50 60 MISAVFGKRR SLSRTLTAGT ICAALISGYA TMASADDGQG ATGEAIIHAD DHPGNWMTYG 70 80 90 100 110 120 RTYSDQRYSP LDQINRSNVG NLKLAWYLDL DTNRGQEGTP LVIDGVMYAT TNWSMMKAVD 130 140 150 160 170 180 AATGKLLWSY DPRVPGNIAD KGCCDTVNRG AAYWNGKVYF GTFDGRLIAL DAKTGKLVWS 190 200 210 220 230 240 VNTIPPEAEL GKQRSYTVDG APRIAKGRVI IGNGGSEFGA RGFVSAFDAE TGKVDWRFFT 250 260 270 280 290 300 VPNPKNEPDA ASDSVLMNKA YQTWSPTGAW TRQGGGGTVW DSIVYDPVAD LVYLGVGNGS 310 320 330 340 350 360 PWNYKYRSEG KGDNLFLGSI VALKPETGEY VWHFQETPMD QWDFTSDQQI MTLDLPINGE 370 380 390 400 410 420 TRHVIVHARK NGFFYIIDAK TGEFISGKNY VYVNWASGLD PKTGRPIYNP DALYTLTGKE 430 440 450 460 470 480 WYGIPGDLGG HNFAAMAFSP KTGLVYIPAQ QVPFLYTNQV GGFTPHPDSW NLGLDMNKVG 490 500 510 520 530 540 IPDSPEAKQA FVKDLKGWIV AWDPQKQAEA WRVDHKGPWN GGILATGGDL LFQGLANGEF 550 560 570 580 590 600 HAYDATNGSD LFHFAADSGI IAPPVTYLAN GKQYVAVEVG WGGIYPFFLG GLARTSGWTV 610 620 630 640 650 660 NHSRIIAFSL DGKSGPLPKQ NDQGFLPVKP PAQFDSKRTD NGYFQFQTYC AACHGDNAEG 670 680 690 700 710 720 AGVLPDLRWS GSIRHEDAFY NVVGRGALTA YGMDRLHGNM NPTEIEDIRQ FLIKRANETY 730 QREVDARKNA DGIPEQLP

References

[1]

"Cloning and sequencing of the gene cluster encoding two subunits of membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes." Tamaki T., Fukaya M., Takemura H., Tayama K., Okumura H., Kawamura Y., Nishiyama M., Horinouchi S., Beppu T. Biochim. Biophys. Acta 1088:292-300(1991) [PubMed: 2001402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 267-279 AND 389-401, FUNCTION. Strain: NBI1028.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00635 Genomic DNA. Translation: BAA00528.1.
PIR	S14270.
3D structure databases
ProteinModelPortal	P28036.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR009056. Cyt_c_dom. IPR003088. Cyt_c_I. IPR019556. PQQ-dependent_C. IPR019551. PQQ-dependent_N. IPR018391. PQQ_beta_propeller_repeat. IPR017512. PQQ_MeOH/EtOH_DH. IPR002372. PQQ_repeat. IPR011047. Quinonprotein_ADH-like. IPR001479. Quinoprotein_DH_CS. [Graphical view]
Gene3D	G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit. G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 1 hit.
Pfam	PF00034. Cytochrom_C. 1 hit. PF01011. PQQ. 4 hits. PF10535. PQQ_C. 1 hit. PF10527. PQQ_N. 1 hit. [Graphical view]
SMART	SM00564. PQQ. 6 hits. [Graphical view]
SUPFAM	SSF46626. Cytochrome_c. 1 hit. SSF50998. Quin_alc_DH_like. 1 hit.
TIGRFAMs	TIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITE	PS00363. BACTERIAL_PQQ_1. 1 hit. PS00364. BACTERIAL_PQQ_2. 1 hit. PS51007. CYTC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHET_ACEPO

Accession

Primary (citable) accession number: P28036

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	July 27, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program