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Protein

Anaerobic glycerol-3-phosphate dehydrogenase subunit A2

Gene

gpdA2

Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conversion of glycerol 3-phosphate to dihydroxyacetone phosphate. Functional analog of glpA1 required for the basal levels of glycerol-3-phosphate dehydrogenase activity, but not expressed during standard growth on glycerol or when glpA1 is knockout.1 Publication

Catalytic activityi

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarity
  • FMNBy similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi4 – 3229FADSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. FMN binding Source: InterPro
  3. sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycerol-3-phosphate metabolic process Source: InterPro
  2. glycerol catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciHVOL309800:GCOK-3291-MONOMER.
UniPathwayiUPA00618; UER00673.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaerobic glycerol-3-phosphate dehydrogenase subunit A2 (EC:1.1.5.3)
Short name:
G-3-P dehydrogenase A2
Short name:
G3PDH A2
Gene namesi
Name:gpdA2
Ordered Locus Names:HVO_A0269
Encoded oniPlasmid pHV40 Publication
OrganismiHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Taxonomic identifieri309800 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax
ProteomesiUP000008243 Componenti: Plasmid pHV4

Subcellular locationi

  1. Cell membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: InterPro
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 563563Anaerobic glycerol-3-phosphate dehydrogenase subunit A2PRO_0000428860Add
BLAST

Interactioni

Subunit structurei

Composed of a catalytic GlpA/B dimer and of membrane bound GlpC.By similarity

Structurei

3D structure databases

ProteinModelPortaliD4GQU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000004814.
KOiK00111.
OMAiCESAGHR.

Family and domain databases

InterProiIPR007419. BFD-like_2Fe2S-bd_dom.
IPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
IPR017752. G3P_DH_GlpA_su.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF04324. Fer2_BFD. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
TIGRFAMsiTIGR03377. glycerol3P_GlpA. 1 hit.
PROSITEiPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D4GQU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYSVVVIGG GATGTGTARD LAMRGFDVTL VERGNLTEGT TGRTHGHLHS
60 70 80 90 100
GARYAVSDKE SAVDCMRENR VLHRIAGHCI EDTGGLFVQL EGDSDDYFER
110 120 130 140 150
KLAGCAECDI PTEVISGEEA RRREPYLTDA VERAIWVPDG AVDPFRLCVA
160 170 180 190 200
NAASAVEHGA RIETHAEVVD LVVEGGRVAG VEVKRQGPNH HSEGAAGDTE
210 220 230 240 250
TFEADYVVSA TGAWAGQLAA MAGVDLEMAI SKGAMVVTNV RQLDTVINRC
260 270 280 290 300
LPKGEGDTII PHETTVLLGA NDDPVDDPDD YPEEQWEVDM MIDIASEMVP
310 320 330 340 350
VVADARMIRA YWGVRPLYDP NPKSTTDPGD VTRNYFVLDH AERDGVAGFA
360 370 380 390 400
SVVGGKLTTY REMAESVSDH VCEVLGVEEP CRTDEVPLPG SADPSALDEY
410 420 430 440 450
MDEFDLRSPI ARRSGQRLGD RAPEVLDIDE PNPTLCECEA VTRAEVRDAI
460 470 480 490 500
DQVGADLNGV RLRTRASMGN CQGGFCSHRL GAELYPDHGA EVARDAVDEL
510 520 530 540 550
YQERWKGQRH ALWGEQLSQA MLNAMLHATT MNHDANHVAG DENIEYRAFD
560
GGRTAVPEGS HGD
Length:563
Mass (Da):60,955
Last modified:May 18, 2010 - v1
Checksum:i50F390554781ED4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001955 Genomic DNA. Translation: ADE02027.1.
RefSeqiYP_003533725.1. NC_013966.1.

Genome annotation databases

EnsemblBacteriaiADE02027; ADE02027; HVO_A0269.
GeneIDi8923720.
KEGGihvo:HVO_A0269.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001955 Genomic DNA. Translation: ADE02027.1.
RefSeqiYP_003533725.1. NC_013966.1.

3D structure databases

ProteinModelPortaliD4GQU6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADE02027; ADE02027; HVO_A0269.
GeneIDi8923720.
KEGGihvo:HVO_A0269.

Phylogenomic databases

HOGENOMiHOG000004814.
KOiK00111.
OMAiCESAGHR.

Enzyme and pathway databases

UniPathwayiUPA00618; UER00673.
BioCyciHVOL309800:GCOK-3291-MONOMER.

Family and domain databases

InterProiIPR007419. BFD-like_2Fe2S-bd_dom.
IPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
IPR017752. G3P_DH_GlpA_su.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF04324. Fer2_BFD. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
TIGRFAMsiTIGR03377. glycerol3P_GlpA. 1 hit.
PROSITEiPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
  2. "Activity and transcriptional regulation of bacterial protein-like glycerol-3-phosphate dehydrogenase of the haloarchaea in Haloferax volcanii."
    Rawls K.S., Martin J.H., Maupin-Furlow J.A.
    J. Bacteriol. 193:4469-4476(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
    Strain: DS2 / DS70.

Entry informationi

Entry nameiGLPA2_HALVD
AccessioniPrimary (citable) accession number: D4GQU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 14, 2014
Last sequence update: May 18, 2010
Last modified: April 29, 2015
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

H.volcanii contains 2 glpABC operons, one located on the main chromosome and the other on megaplasmid pHV4.1 Publication

Keywords - Technical termi

Complete proteome, Plasmid, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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.