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Protein

Uncharacterized lactate 2-monooxygenase PB1A11.03

Gene

SPAPB1A11.03

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-lactate + O2 = acetate + CO2 + H2O.

Cofactori

FMNPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541SubstratePROSITE-ProRule annotation
Binding sitei136 – 1361FMNPROSITE-ProRule annotation
Binding sitei158 – 1581FMNPROSITE-ProRule annotation
Binding sitei160 – 1601SubstratePROSITE-ProRule annotation
Binding sitei188 – 1881FMNPROSITE-ProRule annotation
Binding sitei197 – 1971SubstratePROSITE-ProRule annotation
Binding sitei277 – 2771FMNPROSITE-ProRule annotation
Active sitei301 – 3011Proton acceptorPROSITE-ProRule annotation
Binding sitei304 – 3041SubstratePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi332 – 35625FMNPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular response to oxidative stress Source: PomBase
  • lactate metabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

ReactomeiREACT_348868. Glyoxylate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Uncharacterized lactate 2-monooxygenase PB1A11.03 (EC:1.13.12.4)
Gene namesi
ORF Names:SPAPB1A11.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAPB1A11.03.
PomBaseiSPAPB1A11.03.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • mitochondrial intermembrane space Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Uncharacterized lactate 2-monooxygenase PB1A11.03PRO_0000316582Add
BLAST

Proteomic databases

MaxQBiQ9HDX2.

Interactioni

Protein-protein interaction databases

BioGridi279823. 1 interaction.
MINTiMINT-4702677.
STRINGi4896.SPAPB1A11.03-1.

Structurei

3D structure databases

ProteinModelPortaliQ9HDX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 406379FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1304.
HOGENOMiHOG000217463.
InParanoidiQ9HDX2.
OMAiAVEYGMQ.
OrthoDBiEOG7M3J8P.
PhylomeDBiQ9HDX2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HDX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRNYNWFDA KEPISYESEI YAKGLKFQRP QITVDGRHWE QLAVERMTKD
60 70 80 90 100
AAGYVYGCAG KRETYDKNME SFKKWSIIPN RLIKSGFPDL STTVFGQKYP
110 120 130 140 150
FPIALAPVGV QKIFNPEGES GSCAAATREH IPYIISTASA TSFEDIEKAS
160 170 180 190 200
GPGERWYQLY WPSNDHQDIT ISLLNRAKKT GCRVLIVTLD TFILGWRPSD
210 220 230 240 250
MDNGYDPFLN PDSIGVEHGF SDPVFRKQFK EKHGVEVEEN MLEAAKEFAG
260 270 280 290 300
IVFPGISHDW EDLKFLRKHW DGPIVLKGIM NVPDAKKAVE YGMQGIVVSN
310 320 330 340 350
HGGRQQDGGV ASLTMLPKIV DAVGDKLDVL FDSGVRSGAD IAKALALGAK
360 370 380 390 400
MVLIGRPYVY GLALEGSSGV SHVIRCLLGD LELTLHLSGI VSVKPKDLNR

DVLYKEE
Length:407
Mass (Da):45,311
Last modified:March 1, 2001 - v1
Checksum:iB0039309D1093CA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC19728.1.
RefSeqiNP_593999.1. NM_001019425.2.

Genome annotation databases

EnsemblFungiiSPAPB1A11.03.1; SPAPB1A11.03.1:pep; SPAPB1A11.03.
GeneIDi2543401.
KEGGispo:SPAPB1A11.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC19728.1.
RefSeqiNP_593999.1. NM_001019425.2.

3D structure databases

ProteinModelPortaliQ9HDX2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279823. 1 interaction.
MINTiMINT-4702677.
STRINGi4896.SPAPB1A11.03-1.

Proteomic databases

MaxQBiQ9HDX2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAPB1A11.03.1; SPAPB1A11.03.1:pep; SPAPB1A11.03.
GeneIDi2543401.
KEGGispo:SPAPB1A11.03.

Organism-specific databases

EuPathDBiFungiDB:SPAPB1A11.03.
PomBaseiSPAPB1A11.03.

Phylogenomic databases

eggNOGiCOG1304.
HOGENOMiHOG000217463.
InParanoidiQ9HDX2.
OMAiAVEYGMQ.
OrthoDBiEOG7M3J8P.
PhylomeDBiQ9HDX2.

Enzyme and pathway databases

ReactomeiREACT_348868. Glyoxylate metabolism.

Miscellaneous databases

NextBioi20804416.
PROiQ9HDX2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 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. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYKN3_SCHPO
AccessioniPrimary (citable) accession number: Q9HDX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 85 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.