(data stored in ACNUC16935 zone)

SWISSPROT: HOGA1_EMENI

ID   HOGA1_EMENI             Reviewed;         309 AA.
AC   Q5BD77; C8VMN4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 73.
DE   RecName: Full=Probable 4-hydroxy-2-oxoglutarate aldolase, mitochondrial;
DE            EC=4.1.3.16;
DE   AltName: Full=Dihydrodipicolinate synthase-like;
DE            Short=DHDPS-like protein;
DE   AltName: Full=Probable 2-keto-4-hydroxyglutarate aldolase;
DE            Short=Probable KHG-aldolase;
GN   ORFNames=AN1503;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17258477; DOI=10.1016/j.fgb.2006.12.001;
RA   Kim Y., Nandakumar M.P., Marten M.R.;
RT   "Proteome map of Aspergillus nidulans during osmoadaptation.";
RL   Fungal Genet. Biol. 44:886-895(2007).
CC   -!- FUNCTION: Catalyzes the final step in the metabolic pathway of
CC       hydroxyproline (By similarity). Involved in osmoadaptation.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 4-hydroxy-2-oxoglutarate = pyruvate +
CC       glyoxylate.
CC   -!- ENZYME REGULATION: Inhibited by divalent cations. {ECO:0000250}.
CC   -!- INDUCTION: Down-regulated when grown with elevated levels of
CC       potassium chloride. {ECO:0000269|PubMed:17258477}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
DR   EMBL; AACD01000023; EAA63816.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF84998.1; -; Genomic_DNA.
DR   RefSeq; XP_659107.1; XM_654015.1.
DR   ProteinModelPortal; Q5BD77; -.
DR   SMR; Q5BD77; -.
DR   STRING; 162425.CADANIAP00008128; -.
DR   EnsemblFungi; CADANIAT00008128; CADANIAP00008128; CADANIAG00008128.
DR   EnsemblFungi; EAA63816; EAA63816; AN1503.2.
DR   GeneID; 2874981; -.
DR   KEGG; ani:AN1503.2; -.
DR   HOGENOM; HOG000173607; -.
DR   InParanoid; Q5BD77; -.
DR   OMA; GMDACVP; -.
DR   OrthoDB; EOG092C4H4P; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q5BD77.
DR   SWISS-2DPAGE; Q5BD77.
KW   Complete proteome; Lyase; Reference proteome; Schiff base;
KW   Stress response.
FT   CHAIN         1    309       Probable 4-hydroxy-2-oxoglutarate
FT                                aldolase, mitochondrial.
FT                                /FTId=PRO_0000348285.
FT   REGION       49     50       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    173    173       Schiff-base intermediate with substrate.
FT                                {ECO:0000250}.
FT   SITE        144    144       Involved in proton transfer during
FT                                cleavage. {ECO:0000250}.
SQ   SEQUENCE   309 AA;  32314 MW;  42D3E59113B43F66 CRC64;
     MANRPLVPGV YVPTVAFFAE NEDVDVATVE KHAAYLAKSG VAGIVVQGSN GEAVHLDREE
     RNLITSATRH ALDSVGATSM PVIVGTGAPS TRETINLCKD AAAAGGDYVL VLPPSYYKSL
     VSSAALLDHF RAVADASPIP VLIYNFPGAS AGLDLSSDDI LALSSHPNII GTKLTCGNTG
     KLTRIVAQAG PSFLTFGGSC DFTLQTLIGG GAGVIAGTAN IIPRACVRIM ELYRAGRVEE
     AQKVQAIVAR ADWLAIKGGF VAVKSALQSY RGYGQQPRRP CVAPSSEEAA ALKEAFSESI
     ELERQLESQ
//

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