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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: 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)DescriptionActionsGraphical viewLength
Binding sitei103Substrate1 Publication1
Binding sitei151NADP3 Publications1
Binding sitei177NADP3 Publications1
Binding sitei180NADP3 Publications1
Binding sitei215NADP3 Publications1
Active sitei250PROSITE-ProRule annotation1
Active sitei284PROSITE-ProRule annotation1
Binding sitei377NADP3 Publications1
Binding sitei437Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi230 – 251NADP3 PublicationsAdd BLAST22

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13095.
BRENDAi1.2.1.9. 5941.
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
Proteomesi
  • UP000002512 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000565791 – 475NADP-dependent glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST475

Interactioni

Subunit structurei

Homotetramer.3 Publications

Protein-protein interaction databases

STRINGi210007.SMU_676.

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Beta strandi12 – 14Combined sources3
Beta strandi17 – 23Combined sources7
Turni25 – 27Combined sources3
Beta strandi30 – 35Combined sources6
Helixi39 – 58Combined sources20
Helixi61 – 77Combined sources17
Helixi79 – 90Combined sources12
Helixi94 – 115Combined sources22
Beta strandi120 – 124Combined sources5
Helixi125 – 127Combined sources3
Helixi130 – 132Combined sources3
Beta strandi135 – 143Combined sources9
Beta strandi145 – 150Combined sources6
Beta strandi153 – 155Combined sources3
Helixi158 – 169Combined sources12
Beta strandi173 – 177Combined sources5
Turni180 – 182Combined sources3
Helixi183 – 196Combined sources14
Beta strandi202 – 205Combined sources4
Helixi210 – 219Combined sources10
Beta strandi225 – 230Combined sources6
Helixi232 – 241Combined sources10
Turni242 – 244Combined sources3
Beta strandi247 – 250Combined sources4
Beta strandi255 – 259Combined sources5
Helixi265 – 277Combined sources13
Helixi278 – 281Combined sources4
Beta strandi284 – 293Combined sources10
Helixi294 – 309Combined sources16
Helixi316 – 318Combined sources3
Helixi328 – 343Combined sources16
Beta strandi347 – 350Combined sources4
Beta strandi362 – 366Combined sources5
Helixi372 – 374Combined sources3
Beta strandi380 – 389Combined sources10
Helixi391 – 400Combined sources10
Beta strandi401 – 410Combined sources10
Helixi414 – 423Combined sources10
Beta strandi426 – 433Combined sources8
Beta strandi451 – 453Combined sources3
Helixi457 – 463Combined sources7
Beta strandi465 – 473Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59931.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni154 – 155Substrate binding2
Regioni283 – 285Substrate binding3

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
KOiK00131.
OMAiTEEVDYV.
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)DescriptionActionsGraphical viewLength
Sequence conflicti58S → A in AAA91091 (PubMed:7751269).Curated1
Sequence conflicti85V → I in AAA91091 (PubMed:7751269).Curated1
Sequence conflicti347A → T in AAA91091 (PubMed:7751269).Curated1

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.
WP_002262986.1. 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.
PIRiA57151.
RefSeqiNP_721104.1. NC_004350.2.
WP_002262986.1. NC_004350.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU_676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
KOiK00131.
OMAiTEEVDYV.
PhylomeDBiQ59931.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13095.
BRENDAi1.2.1.9. 5941.
SABIO-RKQ59931.

Miscellaneous databases

EvolutionaryTraceiQ59931.

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]
ProtoNetiSearch...

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 2, 2016
This is version 123 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

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 one 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.