Reviewed, UniProtKB/Swiss-Prot P09972 (ALDOC_HUMAN)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase C
    EC=4.1.2.13
Alternative name(s):
    Brain-type aldolase

Gene names

Name:	ALDOC
Synonyms:	ALDC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	364 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.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subunit structure	Homotetramer.
Miscellaneous	In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.
Sequence similarities	Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	fructose 1,6-bisphosphate metabolic process Inferred from direct assay. Source: UniProtKB glycolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoskeleton Inferred by curator. Source: UniProtKB
Molecular function	cytoskeletal protein binding Inferred from direct assay. Source: UniProtKB fructose-bisphosphate aldolase activity Ref.1 Traceable author statement. Source: ProtInc
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 – 364

363

Fructose-bisphosphate aldolase C

PRO_0000216947

Sites

Active site

188

1

Proton acceptor By similarity

Active site

230

1

Schiff-base intermediate with dihydroxyacetone-P

Binding site

56

1

Substrate

Binding site

147

1

Substrate

Site

364

1

Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue

39

1

Phosphoserine By similarity

Modified residue

119

1

Phosphothreonine By similarity

Modified residue

147

1

N6-acetyllysine

Experimental info

Sequence conflict

311

1

L → V in CAA30270. Ref.2

Secondary structure

1

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364

Helix Strand Turn

Details...

Helix

10 – 23

14

Beta strand

29 – 33

5

Helix

37 – 45

9

Helix

53 – 64

12

Helix

68 – 70

3

Turn

71 – 73

3

Beta strand

74 – 79

6

Helix

82 – 85

4

Helix

94 – 100

7

Beta strand

104 – 108

5

Beta strand

113 – 115

3

Beta strand

119 – 121

3

Beta strand

123 – 125

3

Helix

131 – 140

10

Beta strand

145 – 152

8

Helix

161 – 179

19

Turn

180 – 182

3

Beta strand

184 – 191

8

Helix

199 – 219

21

Helix

224 – 226

3

Helix

246 – 257

12

Turn

258 – 260

3

Beta strand

267 – 271

5

Helix

277 – 288

12

Beta strand

295 – 303

9

Helix

304 – 314

11

Helix

321 – 338

18

Turn

339 – 341

3

Sequences

	Sequence		Length	Mass (Da)
	P09972-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 506A570B3E507971	FASTA	364	39,456
	10 20 30 40 50 60 MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR 70 80 90 100 110 120 QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD 130 140 150 160 170 180 GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ 190 200 210 220 230 240 NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC 250 260 270 280 290 300 PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF 310 320 330 340 350 360 SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA NHAY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete amino acid sequence of the human aldolase C isozyme derived from genomic clones." Rottmann W.H., Deselms K.R., Niclas J., Camerato T., Holman P.S., Green C.J., Tolan D.R. Biochimie 69:137-145(1987) [PubMed: 3105602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete nucleotide sequence of the gene coding for the human aldolase C." Buono P., Paolella G., Mancini F.P., Izzo P., Salvatore F. Nucleic Acids Res. 16:4733-4733(1988) [PubMed: 3267224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Characterization of the transcription-initiation site and of the promoter region within the 5' flanking region of the human aldolase C gene." Buono P., Mancini F.P., Izzo P., Salvatore F. Eur. J. Biochem. 192:805-811(1990) [PubMed: 2209624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	Yu W., Gibbs R.A. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Eye and Uterus.
[8]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, MASS SPECTROMETRY. Tissue: Epithelium.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X05196 Genomic DNA. Translation: CAA28825.1.
X07292 Genomic DNA. Translation: CAA30270.1.
AF054987 mRNA. Translation: AAC09348.1.
BT007006 mRNA. Translation: AAP35652.1.
CR541862 mRNA. Translation: CAG46660.1.
CR541881 mRNA. Translation: CAG46679.1.
BC003613 mRNA. Translation: AAH03613.3.
BC103760 mRNA. Translation: AAI03761.1. Different initiation.
BC065565 mRNA. Translation: AAH65565.2.
BC106925 mRNA. Translation: AAI06926.1.
BC106926 mRNA. Translation: AAI06927.1.

PIR

ADHUC. A25861.

RefSeq

NP_005156.1.

UniGene

Hs.155247

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XFB	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L	1-364	[»]

ModBase

Search...

PTM databases

PhosphoSite

P09972.

Genome annotation databases

Ensembl

ENSG00000109107. Homo sapiens. [Contig view]

GeneID

230.

KEGG

hsa:230.

NMPDR

fig|9606.3.peg.13397.

Organism-specific databases

HGNC

HGNC:418. ALDOC.

HPA

HPA003282.

MIM

103870. gene.

PharmGKB

PA24711.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

P09972.

Enzyme and pathway databases

Reactome

REACT_1709. Metabolism of small molecules.

Gene expression databases

ArrayExpress

P09972.

CleanEx

HS_ALDOC.

GermOnline

ENSG00000109107. Homo sapiens.

Family and domain databases

InterPro

IPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR11627. Aldolase_I. 1 hit.

Pfam

PF00274. Glycolytic. 1 hit.
[Graphical view]

ProDom

PD001128. Aldolase_I. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

934.

SOURCE

Search...

Entry information

Entry name

ALDOC_HUMAN

Accession

Primary (citable) accession number: P09972
Secondary accession number(s): Q3SYL3, Q6FH94, Q6P0L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)