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Protein

Glycerol-3-phosphate dehydrogenase [NAD(P)+]

Gene

gpsA

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881NAD; via amide nitrogenUniRule annotation
Binding sitei88 – 881SubstrateUniRule annotation
Binding sitei120 – 1201NAD; via amide nitrogenUniRule annotation
Active sitei171 – 1711Proton acceptorUniRule annotation
Binding sitei235 – 2351NADUniRule annotation
Binding sitei261 – 2611NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 216NADUniRule annotation

GO - Molecular functioni

  1. glycerol-3-phosphate dehydrogenase [NAD(P)+] activity Source: UniProtKB-HAMAP
  2. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: UniProtKB-EC
  3. glycerol-3-phosphate dehydrogenase [NADP+] activity Source: UniProtKB-EC
  4. NAD binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. glycerol-3-phosphate biosynthetic process Source: UniProtKB-HAMAP
  3. glycerol-3-phosphate catabolic process Source: InterPro
  4. glycerophospholipid metabolic process Source: UniProtKB-UniPathway
  5. phospholipid biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(P)+]UniRule annotation (EC:1.1.1.94UniRule annotation)
Alternative name(s):
NAD(P)H-dependent glycerol-3-phosphate dehydrogenaseUniRule annotation
Gene namesi
Name:gpsAUniRule annotation
Ordered Locus Names:slr1755
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Glycerol-3-phosphate dehydrogenase [NAD(P)+]PRO_0000138047Add
BLAST

Proteomic databases

PaxDbiP73033.

Interactioni

Protein-protein interaction databases

IntActiP73033. 1 interaction.
STRINGi1148.slr1755.

Structurei

3D structure databases

ProteinModelPortaliP73033.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 2362Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0240.
HOGENOMiHOG000246853.
InParanoidiP73033.
KOiK00057.
OMAiAVSIKGV.
OrthoDBiEOG6JDWF4.
PhylomeDBiP73033.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 2 hits.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog.
InterProiIPR008927. 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]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 2 hits.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P73033-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFANADTPP QVVVLGAGAW GSSLAYVLNN NDIPTQVWSR RSPQSLESMV
60 70 80 90 100
AGADVIVSAV SIKGVPSVAA RLEAMDLQRR TILVTATKGL DPETMTTPSQ
110 120 130 140 150
IWQAALPSQP IAVLSGPNLS KEIDQGLPAA TVVASSDQAA AEEIQTIFAA
160 170 180 190 200
DNFRVYTNND PLGTELGGTL KNVMAIAVGV CEGLGLGTNA KSALITRALP
210 220 230 240 250
EITRVGLHFG AQPDTFWGLA GLGDLLATCS SMLSRNYRVG YGLSKGQSLE
260 270 280 290 300
EILANLGGTA EGVNTTDVLI KIANREKIAV PITRQVYRLL HGKITPPQAV
310
EALMERELKA EFEDFDL
Length:317
Mass (Da):33,511
Last modified:June 1, 2001 - v2
Checksum:i1335A86E1B6E0935
GO

Sequence cautioni

The sequence BAA17053.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17053.1. Different initiation.
PIRiS75139.
RefSeqiNP_440373.1. NC_000911.1.
YP_007450257.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA17053; BAA17053; BAA17053.
KEGGisyn:slr1755.
PATRICi23837904. VBISynSp132158_0521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17053.1. Different initiation.
PIRiS75139.
RefSeqiNP_440373.1. NC_000911.1.
YP_007450257.1. NC_020286.1.

3D structure databases

ProteinModelPortaliP73033.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP73033. 1 interaction.
STRINGi1148.slr1755.

Proteomic databases

PaxDbiP73033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17053; BAA17053; BAA17053.
KEGGisyn:slr1755.
PATRICi23837904. VBISynSp132158_0521.

Phylogenomic databases

eggNOGiCOG0240.
HOGENOMiHOG000246853.
InParanoidiP73033.
KOiK00057.
OMAiAVSIKGV.
OrthoDBiEOG6JDWF4.
PhylomeDBiP73033.

Enzyme and pathway databases

UniPathwayiUPA00940.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 2 hits.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog.
InterProiIPR008927. 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]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 2 hits.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.

Entry informationi

Entry nameiGPDA_SYNY3
AccessioniPrimary (citable) accession number: P73033
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.