Reviewed, UniProtKB/Swiss-Prot P17729 (G3P1_TRIKO)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 1
      Short name=GAPDH1
    EC=1.2.1.12

Gene names

Name:

gpd1

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	336 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)-resistant GAPDH isozyme. It is present under antibiotic production.
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-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 336	335	Glyceraldehyde-3-phosphate dehydrogenase 1		PRO_0000145585
Regions
	Nucleotide binding	12 – 13	2	NAD By similarity
	Region	149 – 151	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	209 – 210	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	150	1	Nucleophile By similarity
	Binding site	34	1	NAD By similarity
	Binding site	79	1	NAD; via carbonyl oxygen By similarity
	Binding site	180	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	232	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	314	1	NAD By similarity
	Site	177	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17729-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FC8C87E617297066	FASTA	336	36,252
	10 20 30 40 50 60 MVPKVGINGF GRIGRVVLRN ALETGAVEVV ALNDPFIEPH YAEYMFKYDS THGRFKGDIK 70 80 90 100 110 120 VDGKDLVIDG KRIKFYQERD PANIPWKDSG AEYIVESTGV FTTTEKASAH FKGGAKKVII 130 140 150 160 170 180 SAPSADAPMY VMGVNEDTYA GANVISNASC TTNCLAPLAK TLNDKFTIVE GLMTAIHAYT 190 200 210 220 230 240 ASQKTVDGPS SKDWRGGRAA AQNLIPSSTG AAKAVGKVIP ELAGKVTGMS VRVPTVNVSL 250 260 270 280 290 300 VDFTVRFAKD VTYDEVKAAI KEASEGPLKG ILAYTEDDIV STDILTDPHS STFDAKAGIA 310 320 330 LNKNFVKVMS WYDNEYGYSR RVVDLIVYVS KKDAGQ

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	D14519 mRNA. Translation: BAA03392.1.
PIR	S13205.
3D structure databases
HSSP	HSSP built from PDB template 1IHX based on UniProtKB P56649.
SMR	P17729. Positions 4-335.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.1.12. 97070.
Family and domain databases
InterPro	IPR000173. GlycerAld_3-P_DH. IPR006424. Glyceraldehyde-3-P_DH_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

G3P1_TRIKO

Accession

Primary (citable) accession number: P17729

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)