NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
Nicaud J.-M., le Dall M.-T., Choquer M.;
"Glycerol 3 phosphate dehydrogenase from Yarrowia lipolityca.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CLIB 122 / E 150;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).

Comments

CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD⁺ = glycerone phosphate + NADH.
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ250328; CAB58452.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382128; CAG82664.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_500444.1; -.

3D structure databases

HSSP

P90551; 1EVY. [HSSP ENTRY / PDB]

ModBase

Q9UVF4.

Family and domain databases

InterPro

IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR017751; NAD-dep_Gly3P_DH_euk.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR006109; NAD_Gly3P_DHase_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

PANTHER

PTHR11728; NAD_Gly3P_DH; 1.

Pfam

PF07479; NAD_Gly3P_dh_C; 1.
PF01210; NAD_Gly3P_dh_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000114; Glycerol-3-P_dh; 1.

PRINTS

PR00077; GPDHDRGNASE.

ProDom

PD001278; NAD_Gly3P_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00957; NAD_G3PDH; 1.

BLOCKS

Q9UVF4.

Genome annotation databases

GeneID

2906777; -.

KEGG

yli:YALI0B02948g; -.

Phylogenomic databases

HOGENOM

Q9UVF4; -.

Other

ProtoNet

Q9UVF4.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 398`	`398`	`Glycerol-3-phosphate dehydrogenase [NAD+] 1.`	`PRO_0000138098`
`NP_BIND`	`50 55`	`6`	`NAD (By similarity).`
`REGION`	`318 319`	`2`	`Substrate binding (By similarity).`
`ACT_SITE`	`253 253`		`Proton acceptor (By similarity).`
`BINDING`	`138 138`		`NAD (By similarity).`
`BINDING`	`161 161`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`161 161`		`Substrate (By similarity).`
`BINDING`	`194 194`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`318 318`		`NAD (By similarity).`
`BINDING`	`350 350`		`NAD (By similarity).`

Sequence information

Length: 398 AA [This is the length of the unprocessed precursor]

Molecular weight: 43459 Da [This is the MW of the unprocessed precursor]

CRC64: C576DA65AB076E1E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSALLRSSLR FKHMSAVNRL TQQLRLLTAS APLSAANTAG KAPFKVAVVG SGNWGTTVAK 

        70         80         90        100        110        120 
IVAENCTAHP ELFEPEVRVW VREEKVNGKN LTDIFNAEHE NVRYLPKIKL PHNLIAEPDL 

       130        140        150        160        170        180 
LKAVEGANII VFNLPHQFLA GVCKQLKGHV NPKARAISCL KGLDVTPQGV YLLSDVIENE 

       190        200        210        220        230        240 
TGLHCGVLSG ANLATEIALE KYSETTVAYN RPKDFFGEGD VTNDVLKALF HRPYFHVRCV 

       250        260        270        280        290        300 
QDVAGVSIGG ALKNVVALCA GFVEGKNWGD NAKAAIMRRG MLEMINFSKR FFPETDINTL 

       310        320        330        340        350        360 
TVESAGVADL ITSCAGGRNF KVGRAFGKES GSGKTIQDVE KELLNGQSAQ GVITCNEVHE 

       370        380        390 
LLKNKNMQKD FPLFESTWGI IHGELKIDDL PEILYHAN

Q9UVF4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools