Reviewed, UniProtKB/Swiss-Prot P0A9S1 (FUCO_ECOLI)

Names and origin

Protein names

Recommended name:
    Lactaldehyde reductase
    EC=1.1.1.77
Alternative name(s):
    Propanediol oxidoreductase

Gene names

Name:	fucO
Ordered Locus Names:	b2799, JW2770

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(R)-propane-1,2-diol + NAD+ = (R)-lactaldehyde + NADH. (S)-propane-1,2-diol + NAD+ = (S)-lactaldehyde + NADH.
Cofactor	Iron Potential.
Pathway	Carbohydrate degradation; L-fucose degradation.
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism
Ligand	Iron NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW lactaldehyde reductase 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 – 383

383

Lactaldehyde reductase

PRO_0000087824

Experimental info

Sequence conflict

274

1

N → T in CAA33124. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

383

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Beta strand

10 – 15

6

Helix

18 – 21

4

Helix

22 – 29

8

Beta strand

33 – 37

5

Helix

40 – 44

5

Helix

47 – 57

11

Beta strand

61 – 65

5

Helix

74 – 87

14

Beta strand

90 – 97

8

Helix

98 – 112

15

Helix

114 – 116

3

Helix

120 – 122

3

Beta strand

123 – 125

3

Beta strand

135 – 139

5

Beta strand

141 – 143

3

Turn

146 – 148

3

Beta strand

150 – 156

7

Turn

157 – 160

4

Beta strand

161 – 166

6

Helix

168 – 170

3

Beta strand

173 – 177

5

Helix

179 – 181

3

Turn

182 – 184

3

Helix

187 – 206

20

Helix

212 – 233

22

Helix

237 – 257

21

Helix

261 – 273

13

Helix

277 – 292

16

Helix

293 – 295

3

Helix

299 – 306

8

Helix

316 – 333

18

Helix

340 – 343

4

Helix

347 – 349

3

Helix

350 – 358

9

Helix

361 – 365

5

Sequences

	Sequence		Length	Mass (Da)
	P0A9S1-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: F0103FED90CA33F3	FASTA	383	40,645
	10 20 30 40 50 60 MMANRMILNE TAWFGRGAVG ALTDEVKRRG YQKALIVTDK TLVQCGVVAK VTDKMDAAGL 70 80 90 100 110 120 AWAIYDGVVP NPTITVVKEG LGVFQNSGAD YLIAIGGGSP QDTCKAIGII SNNPEFADVR 130 140 150 160 170 180 SLEGLSPTNK PSVPILAIPT TAGTAAEVTI NYVITDEEKR RKFVCVDPHD IPQVAFIDAD 190 200 210 220 230 240 MMDGMPPALK AATGVDALTH AIEGYITRGA WALTDALHIK AIEIIAGALR GSVAGDKDAG 250 260 270 280 290 300 EEMALGQYVA GMGFSNVGLG LVHGMAHPLG AFYNTPHGVA NAILLPHVMR YNADFTGEKY 310 320 330 340 350 360 RDIARVMGVK VEGMSLEEAR NAAVEAVFAL NRDVGIPPHL RDVGVRKEDI PALAQAALDD 370 380 VCTGGNPREA TLEDIVELYH TAW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol." Chen Y.M., Lu Z., Lin E.C.C. J. Bacteriol. 171:6097-6105(1989) [PubMed: 2553671] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation." Lu Z., Lin E.C.C. Nucleic Acids Res. 17:4883-4884(1989) [PubMed: 2664711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae." Conway T., Ingram L.O. J. Bacteriol. 171:3754-3759(1989) [PubMed: 2661535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Sequencing and characterization of the sdaB gene from Escherichia coli K-12." Shao Z., Newman E.B. Eur. J. Biochem. 212:777-784(1993) [PubMed: 8385012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 353-383. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M31059 Genomic DNA. Translation: AAA23824.1.
X15025 Genomic DNA. Translation: CAA33124.1.
M27177 Genomic DNA. Translation: AAA23825.1.
U29581 Genomic DNA. Translation: AAB40449.1.
U00096 Genomic DNA. Translation: AAC75841.1.
AP009048 Genomic DNA. Translation: BAE76871.1.
L07763 Genomic DNA. No translation available.

PIR

RDECLA. A32883.

RefSeq

AP_003365.1.
NP_417279.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RRM	X-ray	1.60	A/B	1-383	[»]
2BI4	X-ray	2.85	A/B	1-383	[»]
2BL4	X-ray	2.85	A/B	1-383	[»]

ModBase

Search...

Genome annotation databases

GeneID

947273.

GenomeReviews

Gene locus JW2770 in contig AP009048_GR.
Gene locus b2799 in contig U00096_GR.

KEGG

ecj:JW2770.
eco:b2799.

Organism-specific databases

EchoBASE

EB0347.

EcoGene

EG10351. fucO.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9S1.

OMA

P0A9S1. HDIPIVA.

Enzyme and pathway databases

BioCyc

EcoCyc:LACTALDREDUCT-MON.
MetaCyc:LACTALDREDUCT-MON.

Family and domain databases

InterPro

IPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
IPR013460. Lactal_redase.
[Graphical view]

Pfam

PF00465. Fe-ADH. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02638. lactal_redase. 1 hit.

PROSITE

PS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FUCO_ECOLI

Accession

Primary (citable) accession number: P0A9S1
Secondary accession number(s): P11549, Q2MA35

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 37 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)