ID M7P2W7_PNEMU Unreviewed; 1025 AA.
AC M7P2W7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN ORFNames=PNEG_03370 {ECO:0000313|EMBL:EMR08200.1};
OS Pneumocystis murina (strain B123) (Mouse pneumocystis pneumonia agent)
OS (Pneumocystis carinii f. sp. muris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1069680 {ECO:0000313|EMBL:EMR08200.1, ECO:0000313|Proteomes:UP000011958};
RN [1] {ECO:0000313|Proteomes:UP000011958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B123 {ECO:0000313|Proteomes:UP000011958};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00037426}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006936}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMR08200.1}.
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DR EMBL; AFWA02000017; EMR08200.1; -; Genomic_DNA.
DR RefSeq; XP_007875453.1; XM_007877262.1.
DR AlphaFoldDB; M7P2W7; -.
DR STRING; 1069680.M7P2W7; -.
DR GeneID; 19897057; -.
DR VEuPathDB; FungiDB:PNEG_03370; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_1_1; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000011958; Unassembled WGS sequence.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011958};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 655..865
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1025 AA; 117816 MW; 8C82E375F97FFF1C CRC64;
MGRNIYFFQK KILNITKNPF FTKKKDTWKC INTAGRSIKR IHSIAFLKKA PEWSDSFLHG
TSANYIDAMY EVWKKNPEDV HVSWQIYFKN MSNKNIKPIY AFQPPTTIIP ASIGEIPTLP
TGMDDSASII QHLKVQLLVR AYQVRGHLCA DIDPLGIKAK DDLIKEIPKE LTLEYYGFTE
KDLNTEFNLG PGILPAFSTK EESKMTLFSI VENLKRLYSG SYGVEYVHIP DRYQCNWLRE
RLEIPIPYQY NNEEKQRILD RLIWSDSFEK FLATKYPNDK RFGLEGCESL IPGMKALIDH
SVDLGIESIV IGMAHRGRLN VLSNVVKKPN ESIFSEFLGS LDPDSEGSGD VKYHLGMNYE
RPTPSGKRVY LSLVANPSHL EAKDPVVLGQ TRAIQFYAND EQEHSKSMSI LLHGDAAFAA
QGVVYETMGF HSLPKYSTGG TIHLIINNQI GFTTDPRFAR STPYCSDIAK SIDAPIFHVN
GDDVEALVFI CKIASEWRAT FKKDVVIDIV CYRRHGHNET DQPSFTQPLM YRKIIEQTST
LEKYAKQLIK EGSFSEKDIN EHKKCVWDIL ESSFKKAKNY KPTSREWLTS AWNGFASPRD
LTVKNFPHLP TSVDKETLKN LGRKIFLYPK DFNIHPNLKR IIRNRALSIE EEKNIDWATG
EALAFATLLM EGCHVRLSGQ DVERGTFSQR HAVLHDQENE DTYIPLNFID PKQAKFVISN
SSLSEFGVLG FEYGYSLISP NSLVVWEAQF GDFANNAQCI IDQFIASAEV KWRQRSGIIL
SLPHGYDGQG PEHSSGRIER YLQLVNDDYR VFPSKERLQR QHQECNIQIA YPTTPANLFH
LLRRQIHREF RKPLIMFFSK SLLRHPLACS NLSEFSQNSH FQRILDDPGH ENGFLKPREL
CNKLILCTGQ IYVSLYKERQ ERKINDTAIV RCEQIHPFHF QGLKECLDSY PNLKELIWCQ
EEPLNAGAWQ YIQPRLKTVL RETQVHKNKK IKYVGRLPSA SVATGNKIQH KQEHEELIRN
AFESL
//
