Q58813 (FUCA_METJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-fuculose phosphate aldolase
EC=4.1.2.17

Alternative name(s):
L-fuculose-1-phosphate aldolase

Gene names

Name:	fucA
Ordered Locus Names:	MJ1418

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible aldol cleavage of L-fuculose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. The substrate preference order is glyceraldehyde > DL-lactaldehyde, glycolaldehyde > acrolein > formaldehyde, methylglyoxal > acetaldehyde > crotonaldehyde. No activity was observed towards propionaldehyde. Ref.2
Catalytic activity	L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. Ref.2
Cofactor	Binds 1 zinc ion per subunit Potential.
Pathway	Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 3/3. Cofactor biosynthesis; coenzyme F420 biosynthesis.
Subunit structure	Homotetramer. Ref.2
Sequence similarities	Belongs to the aldolase class II family. AraD/FucA subfamily.
Biophysicochemical properties	Kinetic parameters: Vmax=570 nmol/min/mg enzyme with glyceraldehyde as substrate (at pH 7.4 and at 70 degrees Celsius) Ref.2 Vmax=501 nmol/min/mg enzyme with DL-lactaldehyde as substrate (at pH 7.4 and at 70 degrees Celsius)

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fucose catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	L-fuculose-phosphate aldolase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 181	181	L-fuculose phosphate aldolase		PRO_0000162932
Sites
	Metal binding	68	1	Zinc By similarity
	Metal binding	87	1	Zinc By similarity
	Metal binding	89	1	Zinc By similarity
	Metal binding	147	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q58813 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E5F3BF13722145B0	FASTA	181	20,470
	10 20 30 40 50 60 MDKKQFIKIC RKLYDRKYVV GSGGNVSVKE GDKIYLTPTG SILGFLKEDD IAEMDLDGNV 70 80 90 100 110 120 IKGKPTSEKN LHLMIYRKRN DINAIIHTHS LISTFLSTIN KEIELLTPEG KIFLKKIGYV 130 140 150 160 170 180 DYYEAGSLKL AEETAKRDED VIILKNHGVV CLGKDLIDAY IKVEVLEEQA KLTLLNLLVK K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in production of lactate for F420 biosynthesis." Grochowski L.L., Xu H., White R.H. J. Bacteriol. 188:2836-2844(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN F420 BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB99428.1.
PIR	A64477.
RefSeq	NP_248422.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58813.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ1418.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB99428; AAB99428; MJ_1418.
GeneID	1452322.
KEGG	mja:MJ_1418.
Phylogenomic databases
eggNOG	COG0235.
KO	K01628.
OMA	MLPEIDP.
ProtClustDB	CLSK876567.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12176.
UniPathway	UPA00071. UPA00563; UER00626.
Family and domain databases
Gene3D	3.40.225.10. 1 hit.
InterPro	IPR001303. Aldolase_II/adducin_N. [Graphical view]
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
SMART	SM01007. Aldolase_II. 1 hit. [Graphical view]
SUPFAM	SSF53639. Aldolase_II_N. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FUCA_METJA

Accession

Primary (citable) accession number: Q58813

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program