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Protein

Fructose-bisphosphate aldolase

Gene

ald

Organism
Leishmania mexicana
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.UniRule annotationSAAS annotation

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotationSAAS annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (PGI)
  3. no protein annotated in this organism
  4. Fructose-bisphosphate aldolase (ald)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyaseUniRule annotationSAAS annotationImported
Biological processGlycolysisUniRule annotationSAAS annotation
LigandSchiff baseSAAS annotation

Enzyme and pathway databases

BRENDAi4.1.2.13. 2951.
SABIO-RKiQ9U5N6.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolaseUniRule annotationSAAS annotation (EC:4.1.2.13UniRule annotationSAAS annotation)
Gene namesi
Name:aldImported
OrganismiLeishmania mexicanaImported
Taxonomic identifieri5665 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4509.

Interactioni

Protein-protein interaction databases

ELMiQ9U5N6.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EPXX-ray1.80A/B/C/D1-370[»]
2QAPX-ray1.59A/B/C/D1-371[»]
2QDGX-ray2.20A/B/C/D1-371[»]
2QDHX-ray1.90A/B/C/D1-371[»]
ProteinModelPortaliQ9U5N6.
SMRiQ9U5N6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9U5N6.

Family & Domainsi

Sequence similaritiesi

Belongs to the class I fructose-bisphosphate aldolase family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG1557. Eukaryota.
COG3588. LUCA.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiView protein in InterPro
IPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
PfamiView protein in Pfam
PF00274. Glycolytic. 1 hit.
PROSITEiView protein in PROSITE
PS00158. ALDOLASE_CLASS_I. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9U5N6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVTVLQSQ LPAYNRLKTP YESELIATVK KLTTPGKGLL AADESIGSCT
60 70 80 90 100
KRFQPIGLSN TEEHRRQYRA LMLEAEGFEQ YISGVILHDE TVGQKASNGQ
110 120 130 140 150
TFPEYLTARG VVPGIKTDMG LCPLLEGAEG EQMTEGLDGY VKRASAYYKK
160 170 180 190 200
GCRFCKWRNV YKIQNGTVSE SAVRFNAETL ARYAILSQMS GLVPIVEPEV
210 220 230 240 250
MIDGKHDIDT CQRVSEHVWR EVVAALQRHG VIWEGCLLKP NMVVPGAESG
260 270 280 290 300
KTAAPEQVAH YTVMTLARTM PAMLPGVMFL SGGLSEVQAS EYLNAINNSP
310 320 330 340 350
LPRPYFLSFS YARALQSSAL KAWGGKESGL AAGRRAFLHR ARMNSMAQLG
360 370
KYKRSDDDAS SSSLYVKGNT Y
Length:371
Mass (Da):40,837
Last modified:May 1, 2000 - v1
Checksum:i4EE4D9CDFA9126DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243322 Genomic DNA. Translation: CAB55315.1.

Similar proteinsi

Entry informationi

Entry nameiQ9U5N6_LEIME
AccessioniPrimary (citable) accession number: Q9U5N6
Entry historyiIntegrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: August 30, 2017
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources