O22216 (GPDHC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)] GPDHC1, cytosolic
EC=1.1.1.8

Gene names

Name:	GPDHC1
Ordered Locus Names:	At2g41540

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Involved in cell redox homeostasis. Required for maintaining a steady state cellular NADH/NAD+ ratio through a mitochondrial glycerol-3-phosphate redox shuttle. May function with the mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase SDP6 to shuttle reducing equivalents into the mitochondria for respiration. Ref.1
Catalytic activity	sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.
Subcellular location	Cytoplasm › cytosol By similarity.
Tissue specificity	Expressed in roots, leaves, flowers and siliques. Ref.1
Induction	By abscisic acid and salt and dehydration treatments. Down-regulated by hypoxia. Ref.1
Disruption phenotype	No visible phenotype under normal growth conditions, but mutant plants have increased NADH/NAD+ ratios, decreased levels of glycerol-3-phosphate, and produce constitutive high levels of reactive oxygen species (ROS). Ref.1
Sequence similarities	Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay Ref.1. Source: TAIR glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Traceable author statement Ref.1. Source: TAIR glycerol-3-phosphate dehydrogenase [NAD+] activity Inferred from genetic interaction Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Glycerol-3-phosphate dehydrogenase [NAD(+)] GPDHC1, cytosolic		PRO_0000420176
Regions
	Nucleotide binding	48 – 53	6	NAD By similarity
	Region	347 – 348	2	Substrate binding By similarity
Sites
	Active site	285	1	Proton acceptor By similarity
	Binding site	196	1	NAD; via amide nitrogen By similarity
	Binding site	196	1	Substrate By similarity
	Binding site	235	1	NAD; via amide nitrogen By similarity
	Binding site	347	1	NAD By similarity
	Binding site	375	1	NAD By similarity
Experimental info
	Sequence conflict	316	1	E → G in BAH20028. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O22216 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: AD40AF1F464C4908	FASTA	462	51,491
	10 20 30 40 50 60 MVGSIEAKSL QSNGSVHHIG LNLEEKLDEF RRLLGKSEKD PLRIVSVGAG AWGSVFAALL 70 80 90 100 110 120 QESYGGFRDK FQIRIWRRAG RAVDRETAEH LFEVINSRED ILRRLIRRCA YLKYVEARLG 130 140 150 160 170 180 DRTLYADEIL KDGFCLNMVD TPLCPLKVVT NLQEAVWDAD IVVNGLPSTE TREVFEEISK 190 200 210 220 230 240 YWKERITVPI IISLSKGIET ALEPVPHIIT PTKMIHQATG VPIDNVLYLG GPNIAAEIYN 250 260 270 280 290 300 KEYANARICG AAKWRKPLAK FLRQPHFIVW DNSDLVTHEV MGGLKNVYAI GAGMVAALTN 310 320 330 340 350 360 ESATSKSVYF AHCTSEMIFI THLLAEEPEK LAGPLLADTY VTLLKGRNAW YGQMLAKGEI 370 380 390 400 410 420 NRDMGDSISG KGMIQGVSAV GAFYQLLSQS SLSILPSEEK KPVAPVESCP ILKTLYKILI 430 440 450 460 TREQSTQAIL QALRDETLND PRDRIEIAQS HAFYRPSLLG QP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Involvement of a glycerol-3-phosphate dehydrogenase in modulating the NADH/NAD+ ratio provides evidence of a mitochondrial glycerol-3-phosphate shuttle in Arabidopsis." Shen W., Wei Y., Dauk M., Tan Y., Taylor D.C., Selvaraj G., Zou J. Plant Cell 18:422-441(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs." Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K. DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. Tissue: Rosette leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ347019 mRNA. Translation: CAC69665.1. AC002510 Genomic DNA. Translation: AAB84336.1. CP002685 Genomic DNA. Translation: AEC09996.1. CP002685 Genomic DNA. Translation: AEC09997.1. CP002685 Genomic DNA. Translation: AEC09998.1. AY063920 mRNA. Translation: AAL36276.1. AY091247 mRNA. Translation: AAM14186.1. AK317356 mRNA. Translation: BAH20028.1.
IPI	IPI00527775.
PIR	T00810.
RefSeq	NP_001031525.1. NM_001036448.2. NP_181685.1. NM_129717.4. NP_850352.1. NM_180021.4.
UniGene	At.21264. At.69847.
3D structure databases
ProteinModelPortal	O22216.
SMR	O22216. Positions 42-419.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G41540.3-P.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G41540.1; AT2G41540.1; AT2G41540. AT2G41540.2; AT2G41540.2; AT2G41540. AT2G41540.3; AT2G41540.3; AT2G41540.
GeneID	818752.
KEGG	ath:AT2G41540.
Organism-specific databases
TAIR	At2g41540.
Phylogenomic databases
InParanoid	O22216.
OMA	QMISSAT.
PhylomeDB	O22216.
ProtClustDB	CLSN2683781.
Enzyme and pathway databases
BRENDA	1.1.1.8. 302.
Gene expression databases
ArrayExpress	O22216.
Genevestigator	O22216.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit. 3.40.50.720. 1 hit.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013328. DH_multihelical. IPR006168. G3P_DH_NAD-dep. IPR006109. G3P_DH_NAD-dep_C. IPR011128. G3P_DH_NAD-dep_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11728. PTHR11728. 1 hit.
Pfam	PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view]
PRINTS	PR00077. GPDHDRGNASE.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GPDHC_ARATH

Accession

Primary (citable) accession number: O22216
Secondary accession number(s): B9DH11

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program