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Protein

Putative aldehyde dehydrogenase-like protein C9E9.09c

Gene

SPAC9E9.09c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei171 – 1711Transition state stabilizerBy similarity
Active sitei270 – 2701Proton acceptorPROSITE-ProRule annotation
Active sitei304 – 3041NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi247 – 2526NADBy similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: PomBase
  2. aldehyde dehydrogenase [NAD(P)+] activity Source: PomBase

GO - Biological processi

  1. acetate biosynthetic process Source: PomBase
  2. ethanol catabolic process Source: PomBase
  3. NADPH regeneration Source: PomBase
  4. pyruvate metabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Putative aldehyde dehydrogenase-like protein C9E9.09c (EC:1.2.1.-)
Gene namesi
ORF Names:SPAC9E9.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC9E9.09c.
PomBaseiSPAC9E9.09c.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. Golgi apparatus Source: PomBase
  4. mitochondrial matrix Source: PomBase
  5. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Putative aldehyde dehydrogenase-like protein C9E9.09cPRO_0000056595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481Phosphoserine1 Publication
Modified residuei501 – 5011Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14293.
PaxDbiO14293.

Interactioni

Protein-protein interaction databases

BioGridi279414. 66 interactions.
MINTiMINT-4672040.
STRINGi4896.SPAC9E9.09c-1.

Structurei

3D structure databases

ProteinModelPortaliO14293.
SMRiO14293. Positions 23-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
InParanoidiO14293.
KOiK00128.
OMAiHLIMEAA.
OrthoDBiEOG7S226Z.
PhylomeDBiO14293.

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.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR015657. Aminobutyraldehyde_DH.
[Graphical view]
PANTHERiPTHR11699:SF46. PTHR11699:SF46. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKLVDHVE ITVPTGKTYI QPVGLFINNQ HVDSVHGGRV KVYSPSTEKL
60 70 80 90 100
ICEVADADEE DVDIAVKVAR AAFQTDAPWR KFSSAQRGRC LSRLADCIEQ
110 120 130 140 150
NLEYLASIET LDNGKSITLA RGDVQAAADC FRYYGGWADK DYGQTIETDI
160 170 180 190 200
KRFAYTRHEP IGVCGQIIPW NFPFLMCAWK IAPAVACGNT IILKTAELTP
210 220 230 240 250
LSALCLTKFV PECGFPPGVI NVLSGDGRRC GNAISSHMDI DKVAFTGSTG
260 270 280 290 300
VGRMVMRAAA SSNLKKVTLE LGGKSPNIVF NDADLDSAAV WTNYGIFYNS
310 320 330 340 350
GQVCCAGSRV YVQEDVYDEF IKRMVAKAKT LKVGDPFAED TFQGAQVSKQ
360 370 380 390 400
QYERIVSYIE SGIAHGAKLE IGGKRHGNLG YFVEPTILSN VTEDMAVGKE
410 420 430 440 450
EIFGPVLAVI KFKTIEEAIR RGNNSTYGLA AGVHTNNITN AIKVSNALEA
460 470 480 490 500
GTVWVNCYNL LHHQIPFGGY KESGIGRELG SYGLTNYTQT KAVHINLGMD

SPI
Length:503
Mass (Da):54,768
Last modified:January 1, 1998 - v1
Checksum:iA7787A2181FB9CD5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti378 – 3781N → Y in BAA13907 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16407.1.
D89246 mRNA. Translation: BAA13907.1.
PIRiT39216.
T43153.
RefSeqiNP_594582.1. NM_001020011.2.

Genome annotation databases

EnsemblFungiiSPAC9E9.09c.1; SPAC9E9.09c.1:pep; SPAC9E9.09c.
GeneIDi2542976.
KEGGispo:SPAC9E9.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16407.1.
D89246 mRNA. Translation: BAA13907.1.
PIRiT39216.
T43153.
RefSeqiNP_594582.1. NM_001020011.2.

3D structure databases

ProteinModelPortaliO14293.
SMRiO14293. Positions 23-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279414. 66 interactions.
MINTiMINT-4672040.
STRINGi4896.SPAC9E9.09c-1.

Proteomic databases

MaxQBiO14293.
PaxDbiO14293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC9E9.09c.1; SPAC9E9.09c.1:pep; SPAC9E9.09c.
GeneIDi2542976.
KEGGispo:SPAC9E9.09c.

Organism-specific databases

EuPathDBiFungiDB:SPAC9E9.09c.
PomBaseiSPAC9E9.09c.

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
InParanoidiO14293.
KOiK00128.
OMAiHLIMEAA.
OrthoDBiEOG7S226Z.
PhylomeDBiO14293.

Miscellaneous databases

NextBioi20804009.
PROiO14293.

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.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR015657. Aminobutyraldehyde_DH.
[Graphical view]
PANTHERiPTHR11699:SF46. PTHR11699:SF46. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-503.
    Strain: PR745.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiYF19_SCHPO
AccessioniPrimary (citable) accession number: O14293
Secondary accession number(s): P78895
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.