P99117 (ALF1_STAAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase class 1
EC=4.1.2.13

Alternative name(s):
Fructose-bisphosphate aldolase class I
Short name=FBP aldolase

Gene names

Name:	fda
Ordered Locus Names:	SA2399

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	296 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)

Catalytic activity	D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. HAMAP-Rule MF_00729
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. HAMAP-Rule MF_00729
Sequence similarities	Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP
Molecular_function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 296	295	Fructose-bisphosphate aldolase class 1 HAMAP-Rule MF_00729		PRO_0000216905
Sites
	Active site	175	1	Proton acceptor By similarity
	Active site	212	1	Schiff-base intermediate with dihydroxyacetone-P By similarity

Sequences

	Sequence		Length	Mass (Da)
	P99117 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: D63B1A3C7646725B	FASTA	296	33,042
	10 20 30 40 50 60 MNKEQLEKMK NGKGFIAALD QSGGSTPKAL KEYGVNEDQY SNEDEMFQLV HDMRTRVVTS 70 80 90 100 110 120 PSFSPDKILG AILFEQTMDR EVEGKYTADY LADKGVVPFL KVDKGLAEEQ NGVQLMKPID 130 140 150 160 170 180 NLDSLLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE VAKQIIAKGL VPIIEPEVNI 190 200 210 220 230 240 NAKDKAEIEK VLKAELKKGL DSLNADQLVM LKLTIPTEPN LYKELAEHPN VVRVVVLSGG 250 260 270 280 290 YSREKANELL KDNDELIASF SRALASDLRA DQSKEEFDKA LGDAVESIYD ASVNKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315.
[2]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315.
[3]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB43704.1.
PIR	F90067.
RefSeq	NP_375725.1. NC_002745.2.
3D structure databases
ProteinModelPortal	P99117.
SMR	P99117. Positions 1-293.
ModBase	Search...
Protein-protein interaction databases
STRING	158879.SA2399.
PTM databases
PhosSite	P0909757.
2D gel databases
SWISS-2DPAGE	P99117.
Proteomic databases
PRIDE	P99117.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB43704; BAB43704; BAB43704.
GeneID	1125328.
KEGG	sau:SA2399.
PATRIC	19577364. VBIStaAur116463_2600.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3588.
HOGENOM	HOG000073502.
KO	K01623.
OMA	GTKMRSV.
ProtClustDB	PRK05377.
Enzyme and pathway databases
BioCyc	SAUR158879:GJCB-2562-MONOMER.
UniPathway	UPA00109; UER00183.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00729. FBP_aldolase_1.
InterPro	IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. IPR023014. FBP_aldolase_I_bac. [Graphical view]
Pfam	PF00274. Glycolytic. 1 hit. [Graphical view]
PROSITE	PS00158. ALDOLASE_CLASS_I. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF1_STAAN

Accession

Primary (citable) accession number: P99117
Secondary accession number(s): Q99R31

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program