O14400 (GPDM_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycerol-3-phosphate dehydrogenase, mitochondrial
Short name=GPD-M
Short name=GPDH-M
EC=1.1.5.3

Gene names

Name:	gut2
ORF Names:	SPCC1223.03c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	649 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
Cofactor	FAD By similarity.
Pathway	Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NADH oxidation Inferred from sequence orthology. Source: PomBase carbohydrate metabolic process Inferred from sequence or structural similarity. Source: PomBase cellular response to stress Inferred from expression pattern PubMed 12529438. Source: PomBase glycerol catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glycerol-3-phosphate metabolic process Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	glycerol-3-phosphate dehydrogenase complex Inferred from sequence orthology. Source: PomBase mitochondrion Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	glycerol-3-phosphate dehydrogenase activity Inferred from sequence orthology. Source: PomBase sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 649		Glycerol-3-phosphate dehydrogenase, mitochondrial		PRO_0000010433
Regions
	Nucleotide binding	69 – 97	29	FAD Potential

Sequences

	Sequence		Length	Mass (Da)
	O14400 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 65702D1FDE831E6A	FASTA	649	71,873
	10 20 30 40 50 60 MFSIFKRRSV QAALAASGLV GGAVFYSDFI KRPAPSHFNP QFTPFTKSLA PPPSRETLLK 70 80 90 100 110 120 NVEDISKFDV LIIGGGATGT GVAVDASTRG LNVCLLEKTD FASETSSKST KMAHGGVRYL 130 140 150 160 170 180 EKAVFQLSKA QLDLVIEALN ERANMLRTAP HLCTVLPIMI PVYKWWQVPY FFVGCKIYDW 190 200 210 220 230 240 VAGSKNLRAS TIFSKETTVA IAPMLDDSNL KASCVYHDGS FNDTRMNTTL AVTAIDNGAT 250 260 270 280 290 300 VLNYMEVKKL LKSKDNKLEG VLAIDRETGK EYQIKATSVV NATGPFSDKI LEMDADPQGE 310 320 330 340 350 360 PPKTAQFPRM VVPSAGVHVV LPEYYCPPNI GILDPSTSDN RVMFFLPWQG KVIAGTTDKP 370 380 390 400 410 420 LSSVPTNPTP SEDDIQLILK ELQKYLVFPV DREDVLSAWC GIRPLVRDPS TVPPGTDPTT 430 440 450 460 470 480 GETQGLVRSH FIFKSDTGLL TISGGKWTTY REMAEETVNE LIKDHDFGKA LKPCQTKKLI 490 500 510 520 530 540 LVGGENYYKN YSARLIHEYH IPLRLAKHLS HNYGSRAPLI LELYSKTDFN KLPVTLADKE 550 560 570 580 590 600 VFAPSSDASS DKSVSYASFD EPFTVAELKY SIKYEYTRTP TDFLARRTRL AFLDARQALQ 610 620 630 640 AVAGVTHVMK EEFGWDDATT DKLAQEARDY IGGMGVSSDR FDVKQFEVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Hansen K. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y14993 Genomic DNA. Translation: CAA75227.1. CU329672 Genomic DNA. Translation: CAA20872.1.
PIR	T40863.
RefSeq	NP_588348.1. NM_001023339.2.
3D structure databases
ProteinModelPortal	O14400.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPCC1223.03c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC1223.03c.1; SPCC1223.03c.1:pep; SPCC1223.03c.
GeneID	2539217.
KEGG	spo:SPCC1223.03c.
Organism-specific databases
PomBase	SPCC1223.03c.
Phylogenomic databases
eggNOG	COG0578.
HOGENOM	HOG000004813.
KO	K00111.
OMA	DSIRKMD.
OrthoDB	EOG46MFT1.
Enzyme and pathway databases
UniPathway	UPA00618; UER00673.
Family and domain databases
InterPro	IPR006076. FAD-dep_OxRdtase. IPR000447. G3P_DH_FAD-dep. [Graphical view]
Pfam	PF01266. DAO. 1 hit. [Graphical view]
PRINTS	PR01001. FADG3PDH.
PROSITE	PS00977. FAD_G3PDH_1. 1 hit. PS00978. FAD_G3PDH_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20800387.

Entry information

Entry name

GPDM_SCHPO

Accession

Primary (citable) accession number: O14400

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program