HOGA1_COCIM
ID HOGA1_COCIM Reviewed; 314 AA.
AC P0CL20; J3KGB9; J3KGD9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Putative 4-hydroxy-2-oxoglutarate aldolase, mitochondrial;
DE EC=4.1.3.16;
DE AltName: Full=Dihydrodipicolinate synthase-like;
DE Short=DHDPS-like protein;
GN ORFNames=CIMG_00151;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- FUNCTION: May catalyze the final step in the metabolic pathway of
CC hydroxyproline. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:71685; EC=4.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC Xref=Rhea:RHEA:30687, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:62213; EC=4.1.3.16;
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG704911; EAS34797.3; -; Genomic_DNA.
DR RefSeq; XP_001246380.1; XM_001246379.2.
DR AlphaFoldDB; P0CL20; -.
DR SMR; P0CL20; -.
DR STRING; 246410.P0CL20; -.
DR EnsemblFungi; EAS34797; EAS34797; CIMG_00151.
DR GeneID; 4566390; -.
DR KEGG; cim:CIMG_00151; -.
DR VEuPathDB; FungiDB:CIMG_00151; -.
DR InParanoid; P0CL20; -.
DR OMA; WCTAAPC; -.
DR OrthoDB; 1238597at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0106009; F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity; IEA:RHEA.
DR GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Lyase; Reference proteome; Schiff base.
FT CHAIN 1..314
FT /note="Putative 4-hydroxy-2-oxoglutarate aldolase,
FT mitochondrial"
FT /id="PRO_0000405774"
FT ACT_SITE 171
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 50..51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 141
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000250"
SQ SEQUENCE 314 AA; 33243 MW; 059803B263EEF45D CRC64;
MVPRVPQPGI WCPAVTFFDS KTDTLDLASQ ERYYAYLARS GLTGLVILGT NAEAFLLTRE
ERAQLIATAR KAVGPDFPIM AGVGAHSTRQ VLEHINDASV AGANYVLVLP PAYFGKATTP
PVIKSFFDDV SCQSPLPVVI YNFPGVCNGI DLDSDMITTI ARKNPNVVGV KLTCASVGKI
TRLAATLPPA AFSVFGGQSD FLIGGLSVGS AGCIAAFANV FPKTVSKIYE LYKAGKVDQA
MELHRKAALA ESPCKSGIAT TKYAAAIFSA KAAGIEDAEE KLRPRKPYDP PSEAAKQEVR
KVMAEVAAIE AGLS