Reviewed, UniProtKB/Swiss-Prot P17730 (G3P2_TRIKO)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
      Short name=GAPDH2
    EC=1.2.1.12

Gene names

Name:

gpd2

Organism

Trichoderma koningii (Hypocrea koningii)

Taxonomic identifier

97093 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Protein attributes

Sequence length	338 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-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
Enzyme regulation	Inhibited by koningic acid through the interaction of cysteine residues with koningic acid even at very low concentrations.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Miscellaneous	This protein is a koningic acid (antibiotic)-sensitive GAPDH isozyme. It is present only when no antibiotic is produced.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 338	337	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145586
Regions
	Nucleotide binding	13 – 14	2	NAD By similarity
	Region	151 – 153	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	211 – 212	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	152	1	Nucleophile By similarity
	Binding site	35	1	NAD By similarity
	Binding site	80	1	NAD; via carbonyl oxygen By similarity
	Binding site	182	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	234	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	316	1	NAD By similarity
	Site	179	1	Activates thiol group during catalysis By similarity
Experimental info
	Sequence conflict	25	1	H → K AA sequence Ref.2
	Sequence conflict	27	1	D → N AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P17730-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5D054CB198A78514	FASTA	338	36,106
	10 20 30 40 50 60 MAPIKVGING FGRIGRIVFR NAVEHPDIEV VAVNDPFIET TYAAYMLKYD SSHGLFKGEV 70 80 90 100 110 120 EVDGKDLVVN GKKVRFYTER NPADIKWSET GAEYVVESTG VFTTTEKAKA HLVGGAKKVI 130 140 150 160 170 180 ISAPSADAPM YVMGVNESDY DGSADVISNA SCTTNCLAPL AKVINDNYGI VEGLMTTVHS 190 200 210 220 230 240 YTATQKTVDG PSAKDWRGGR GAAQNIIPSS TGAAKAVGKV IPALNGKLTG MSIRVPTANV 250 260 270 280 290 300 SVVDLTVRIE KGASYEEITE TIKKAADGPL KGVLAYTGDD VVSSDMLGNT NSSIFDIKAG 310 320 330 ISLNKNFVKL VSWYDNEWGY SRRVLDLLAH VAKVDASK

References

[1]	"Cloning of two isozymes of Trichoderma koningii glyceraldehyde-3-phosphate dehydrogenase with different sensitivity to koningic acid." Watanabe H., Hasumi K., Fukushima Y., Sakai K., Endo A. Biochim. Biophys. Acta 1172:43-48(1993) [PubMed: 8439569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: M3947.
[2]	"Two glyceraldehyde-3-phosphate dehydrogenase isozymes from the koningic acid (heptelidic acid) producer Trichoderma koningii." Sakai K., Hasumi K., Endo A. Eur. J. Biochem. 193:195-202(1990) [PubMed: 2226438] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-32. Strain: M3947.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D14518 mRNA. Translation: BAA03391.1.
3D structure databases
HSSP	HSSP built from PDB template 1CRW based on UniProtKB P56649.
ModBase	Search...
Family and domain databases
InterPro	IPR000173. GlycerAld_3-P_DHase. IPR006424. Glyceraldehyde-3-P_DHase_1. [Graphical view]
PANTHER	PTHR10836. GAP_DH. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P2_TRIKO

Accession

Primary (citable) accession number: P17730

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)