P73033 (GPDA_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(P)+]
EC=1.1.1.94

Alternative name(s):
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase

Gene names

Name:	gpsA
Ordered Locus Names:	slr1755

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › Synechocystis sp. PCC 6803

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP-Rule MF_00394
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP-Rule MF_00394
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Sequence caution	The sequence BAA17053.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
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 biosynthetic process Inferred from electronic annotation. Source: HAMAP glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro glycerophospholipid metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway phospholipid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: HAMAP glycerol-3-phosphate dehydrogenase [NAD+] 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
	Chain	1 – 317	317	Glycerol-3-phosphate dehydrogenase [NAD(P)+] HAMAP-Rule MF_00394		PRO_0000138047
Regions
	Nucleotide binding	16 – 21	6	NAD By similarity
	Region	235 – 236	2	Substrate binding By similarity
Sites
	Active site	171	1	Proton acceptor By similarity
	Binding site	88	1	NAD; via amide nitrogen By similarity
	Binding site	88	1	Substrate By similarity
	Binding site	120	1	NAD; via amide nitrogen By similarity
	Binding site	235	1	NAD By similarity
	Binding site	261	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P73033 [UniParc]. Last modified June 1, 2001. Version 2. Checksum: 1335A86E1B6E0935	FASTA	317	33,511
	10 20 30 40 50 60 MSFANADTPP QVVVLGAGAW GSSLAYVLNN NDIPTQVWSR RSPQSLESMV AGADVIVSAV 70 80 90 100 110 120 SIKGVPSVAA RLEAMDLQRR TILVTATKGL DPETMTTPSQ IWQAALPSQP IAVLSGPNLS 130 140 150 160 170 180 KEIDQGLPAA TVVASSDQAA AEEIQTIFAA DNFRVYTNND PLGTELGGTL KNVMAIAVGV 190 200 210 220 230 240 CEGLGLGTNA KSALITRALP EITRVGLHFG AQPDTFWGLA GLGDLLATCS SMLSRNYRVG 250 260 270 280 290 300 YGLSKGQSLE EILANLGGTA EGVNTTDVLI KIANREKIAV PITRQVYRLL HGKITPPQAV 310 EALMERELKA EFEDFDL

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA17053.1. Different initiation.
PIR	S75139.
RefSeq	NP_440373.1. NC_000911.1. YP_007450257.1. NC_020286.1.
3D structure databases
ProteinModelPortal	P73033.
ModBase	Search...
Protein-protein interaction databases
IntAct	P73033. 1 interaction.
STRING	1148.slr1755.
Proteomic databases
PaxDb	P73033.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA17053; BAA17053; BAA17053.
GeneID	14615905. 953673.
KEGG	syn:slr1755.
PATRIC	23837904. VBISynSp132158_0521.
Phylogenomic databases
eggNOG	COG0240.
HOGENOM	HOG000246853.
KO	K00057.
OMA	KTETFFG.
ProtClustDB	PRK14619.
Enzyme and pathway databases
UniPathway	UPA00940.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit. 3.40.50.720. 2 hits.
HAMAP	MF_00394. NAD_Glyc3P_dehydrog.
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. 2 hits. [Graphical view]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPDA_SYNY3

Accession

Primary (citable) accession number: P73033

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program