Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q59931

- GAPN_STRMU

UniProt

Q59931 - GAPN_STRMU

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (28 Nov 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MTKQYKNYVN GEWKLSENEI KIYEPASGAE LGSVPAMSTE EVDYVYASAK    50
    KAQPAWRSLS YIERAAYLHK VADILMRDKE KIGAVLSKEV AKGYKSAVSE 100
    VVRTAEIINY AAEEGLRMEG EVLEGGSFEA ASKKKIAVVR REPVGLVLAI 150
    SPFNYPVNLA GSKIAPALIA GNVIAFKPPT QGSISGLLLA EAFAEAGLPA 200
    GVFNTITGRG SEIGDYIVEH QAVNFINFTG STGIGERIGK MAGMRPIMLE 250
    LGGKDSAIVL EDADLELTAK NIIAGAFGYS GQRCTAVKRV LVMESVADEL 300
    VEKIREKVLA LTIGNPEDDA DITPLIDTKS ADYVEGLIND ANDKGAAALT 350
    EIKREGNLIC PILFDKVTTD MRLAWEEPFG PVLPIIRVTS VEEAIEISNK 400
    SEYGLQASIF TNDFPRAFGI AEQLEVGTVH INNKTQRGTD NFPFLGAKKS 450
    GAGIQGVKYS IEAMTTVKSV VFDIK 475
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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: October 1, 2014
    This is version 110 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