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Q59931

- GAPN_STRMU

UniProt

Q59931 - GAPN_STRMU

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Protein

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase

Gene

gapN

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031Substrate1 Publication
Binding sitei151 – 1511NADP3 Publications
Binding sitei177 – 1771NADP3 Publications
Binding sitei180 – 1801NADP3 Publications
Binding sitei215 – 2151NADP3 Publications
Active sitei250 – 2501PROSITE-ProRule annotation
Active sitei284 – 2841PROSITE-ProRule annotation
Binding sitei377 – 3771NADP3 Publications
Binding sitei437 – 4371Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi230 – 25122NADP3 PublicationsAdd
BLAST

GO - Molecular functioni

  1. glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13095.
SMUT210007:GC7Z-660-MONOMER.
SABIO-RKQ59931.

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.9)
Alternative name(s):
Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]
Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase
Triosephosphate dehydrogenase
Gene namesi
Name:gapN
Ordered Locus Names:SMU_676
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000002512: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475NADP-dependent glyceraldehyde-3-phosphate dehydrogenasePRO_0000056579Add
BLAST

Interactioni

Subunit structurei

Homotetramer.3 Publications

Protein-protein interaction databases

STRINGi210007.SMU.676.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Beta strandi12 – 143Combined sources
Beta strandi17 – 237Combined sources
Turni25 – 273Combined sources
Beta strandi30 – 356Combined sources
Helixi39 – 5820Combined sources
Helixi61 – 7717Combined sources
Helixi79 – 9012Combined sources
Helixi94 – 11522Combined sources
Beta strandi120 – 1245Combined sources
Helixi125 – 1273Combined sources
Helixi130 – 1323Combined sources
Beta strandi135 – 1439Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi153 – 1553Combined sources
Helixi158 – 16912Combined sources
Beta strandi173 – 1775Combined sources
Turni180 – 1823Combined sources
Helixi183 – 19614Combined sources
Beta strandi202 – 2054Combined sources
Helixi210 – 21910Combined sources
Beta strandi225 – 2306Combined sources
Helixi232 – 24110Combined sources
Turni242 – 2443Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi255 – 2595Combined sources
Helixi265 – 27713Combined sources
Helixi278 – 2814Combined sources
Beta strandi284 – 29310Combined sources
Helixi294 – 30916Combined sources
Helixi316 – 3183Combined sources
Helixi328 – 34316Combined sources
Beta strandi347 – 3504Combined sources
Beta strandi362 – 3665Combined sources
Helixi372 – 3743Combined sources
Beta strandi380 – 38910Combined sources
Helixi391 – 40010Combined sources
Beta strandi401 – 41010Combined sources
Helixi414 – 42310Combined sources
Beta strandi426 – 4338Combined sources
Beta strandi451 – 4533Combined sources
Helixi457 – 4637Combined sources
Beta strandi465 – 4739Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUHX-ray1.82A/B/C/D1-475[»]
1QI1X-ray3.00A/B/C/D1-475[»]
1QI6X-ray2.50A/B/C/D1-475[»]
2ESDX-ray2.55A/B/C/D1-475[»]
2EUHX-ray2.60A/B/C/D1-475[»]
2ID2X-ray2.50A/B/C/D1-475[»]
2QE0X-ray2.19A/B/C/D1-475[»]
ProteinModelPortaliQ59931.
SMRiQ59931. Positions 2-475.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59931.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni154 – 1552Substrate binding
Regioni283 – 2853Substrate binding

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
KOiK00131.
OMAiLIAGEWC.
OrthoDBiEOG6BS8QW.
PhylomeDBiQ59931.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59931-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKQYKNYVN GEWKLSENEI KIYEPASGAE LGSVPAMSTE EVDYVYASAK
60 70 80 90 100
KAQPAWRSLS YIERAAYLHK VADILMRDKE KIGAVLSKEV AKGYKSAVSE
110 120 130 140 150
VVRTAEIINY AAEEGLRMEG EVLEGGSFEA ASKKKIAVVR REPVGLVLAI
160 170 180 190 200
SPFNYPVNLA GSKIAPALIA GNVIAFKPPT QGSISGLLLA EAFAEAGLPA
210 220 230 240 250
GVFNTITGRG SEIGDYIVEH QAVNFINFTG STGIGERIGK MAGMRPIMLE
260 270 280 290 300
LGGKDSAIVL EDADLELTAK NIIAGAFGYS GQRCTAVKRV LVMESVADEL
310 320 330 340 350
VEKIREKVLA LTIGNPEDDA DITPLIDTKS ADYVEGLIND ANDKGAAALT
360 370 380 390 400
EIKREGNLIC PILFDKVTTD MRLAWEEPFG PVLPIIRVTS VEEAIEISNK
410 420 430 440 450
SEYGLQASIF TNDFPRAFGI AEQLEVGTVH INNKTQRGTD NFPFLGAKKS
460 470
GAGIQGVKYS IEAMTTVKSV VFDIK
Length:475
Mass (Da):51,194
Last modified:November 28, 2002 - v2
Checksum:iF0A2770AB89552DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581S → A in AAA91091. (PubMed:7751269)Curated
Sequence conflicti85 – 851V → I in AAA91091. (PubMed:7751269)Curated
Sequence conflicti347 – 3471A → T in AAA91091. (PubMed:7751269)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38521 Genomic DNA. Translation: AAA91091.1.
AE014133 Genomic DNA. Translation: AAN58410.1.
PIRiA57151.
RefSeqiNP_721104.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN58410; AAN58410; SMU_676.
GeneIDi1028095.
KEGGismu:SMU_676.
PATRICi19663537. VBIStrMut61772_0601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38521 Genomic DNA. Translation: AAA91091.1 .
AE014133 Genomic DNA. Translation: AAN58410.1 .
PIRi A57151.
RefSeqi NP_721104.1. NC_004350.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EUH X-ray 1.82 A/B/C/D 1-475 [» ]
1QI1 X-ray 3.00 A/B/C/D 1-475 [» ]
1QI6 X-ray 2.50 A/B/C/D 1-475 [» ]
2ESD X-ray 2.55 A/B/C/D 1-475 [» ]
2EUH X-ray 2.60 A/B/C/D 1-475 [» ]
2ID2 X-ray 2.50 A/B/C/D 1-475 [» ]
2QE0 X-ray 2.19 A/B/C/D 1-475 [» ]
ProteinModelPortali Q59931.
SMRi Q59931. Positions 2-475.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 210007.SMU.676.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN58410 ; AAN58410 ; SMU_676 .
GeneIDi 1028095.
KEGGi smu:SMU_676.
PATRICi 19663537. VBIStrMut61772_0601.

Phylogenomic databases

eggNOGi COG1012.
KOi K00131.
OMAi LIAGEWC.
OrthoDBi EOG6BS8QW.
PhylomeDBi Q59931.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13095.
SMUT210007:GC7Z-660-MONOMER.
SABIO-RK Q59931.

Miscellaneous databases

EvolutionaryTracei Q59931.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence, expression, and function of the gene for the nonphosphorylating, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Streptococcus mutans."
    Boyd D.A., Cvitkovitch D.G., Hamilton I.R.
    J. Bacteriol. 177:2622-2627(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NG5 / Serotype c.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700610 / UA159.
  3. "Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans."
    Cobessi D., Tete-Favier F., Marchal S., Azza S., Branlant G., Aubry A.
    J. Mol. Biol. 290:161-173(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH NADP, HOMOTETRAMERIZATION.
  4. "Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans."
    Cobessi D., Tete-Favier F., Marchal S., Branlant G., Aubry A.
    J. Mol. Biol. 300:141-152(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE.
  5. "Invariant Thr244 is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans."
    Pailot A., D'Ambrosio K., Corbier C., Talfournier F., Branlant G.
    Biochem. J. 400:521-530(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADP, CHARACTERIZATION.

Entry informationi

Entry nameiGAPN_STRMU
AccessioniPrimary (citable) accession number: Q59931
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: November 26, 2014
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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3