Reviewed, UniProtKB/Swiss-Prot P47269 (ALF_MYCGE)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase
      Short name=FBP aldolase
      Short name=FBPA
    EC=4.1.2.13
Alternative name(s):
    Fructose-1,6-bisphosphate aldolase

Gene names

Name:	fba
Synonyms:	tsr
Ordered Locus Names:	MG023

Organism

Mycoplasma genitalium [Complete proteome] [HAMAP]

Taxonomic identifier

2097 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis By similarity.
Catalytic activity	D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
Cofactor	Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fructose 1,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC zinc 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 – 288	288	Fructose-bisphosphate aldolase		PRO_0000178719
Regions
	Region	207 – 209	3	Dihydroxyacetone phosphate binding By similarity
	Region	228 – 231	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	84	1	Proton donor By similarity
	Metal binding	85	1	Zinc 1; catalytic By similarity
	Metal binding	105	1	Zinc 2 By similarity
	Metal binding	135	1	Zinc 2 By similarity
	Metal binding	177	1	Zinc 1; catalytic By similarity
	Metal binding	206	1	Zinc 1; catalytic By similarity
	Binding site	49	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	178	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47269-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: BD09F4683DD6A32F	FASTA	288	31,310
	10 20 30 40 50 60 MLVNFKLMLQ KAKLGKYAIP HININNYEWA KAVLTAANQA NSPIIVSVSE GALKYMSGYS 70 80 90 100 110 120 VVIPLVKGLI ESLSVKVPVT LHLDHGSYDA CIQALQAGFS SVMFDGSHLP FEENFNKSKK 130 140 150 160 170 180 LIEIAQKTNA SVELEVGTIG GEEDGVIGQG ELANVDECKQ IASLKPDALA AGIGNIHGIY 190 200 210 220 230 240 PKNWKGLNFP LIETISKITN LPLVLHGGSG ILENDVKKAI SLGICKLNIN TECQLAFAHE 250 260 270 280 IRKYIESNKD LDLNKKGYDP RKLLKEPTQA IVDTCLEKID LCGSRNKA

References

[1]

"The minimal gene complement of Mycoplasma genitalium." Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., Nguyen D.T., Utterback T.R., Saudek D.M. , Phillips C.A., Merrick J.M., Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C. Science 270:397-403(1995) [PubMed: 7569993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33530 / G-37 / NCTC 10195.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L43967 Genomic DNA. Translation: AAC71239.1.
PIR	E64202.
RefSeq	NP_072683.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	875427.
KEGG	mge:MG_023.
TIGR	MG023.
Phylogenomic databases
HOGENOM	HBG327581.
OMA	IEKIHER.
Enzyme and pathway databases
BioCyc	MGEN243273:MG_023-MON.
BRENDA	4.1.2.13. 110.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR011289. Fruc_bis_ald_. IPR000771. Ketose_bisP_aldolase_II. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01116. F_bP_aldolase. 1 hit. [Graphical view]
PIRSF	PIRSF001359. F_bP_aldolase_II. 1 hit.
PROSITE	PS00602. ALDOLASE_CLASS_II_1. 1 hit. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF_MYCGE

Accession

Primary (citable) accession number: P47269

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	December 15, 2009
This is version 57 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)