ID A0A0L0SKT5_ALLM3 Unreviewed; 1060 AA.
AC A0A0L0SKT5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AMAG_08214 {ECO:0000313|EMBL:KNE63048.1};
OS Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS macrogynus).
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces.
OX NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE63048.1, ECO:0000313|Proteomes:UP000054350};
RN [1] {ECO:0000313|EMBL:KNE63048.1, ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE63048.1,
RC ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Allomyces macrogynus ATCC 38327.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA Lander E., Nusbaum C.;
RT "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; GG745341; KNE63048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0SKT5; -.
DR STRING; 578462.A0A0L0SKT5; -.
DR EnsemblFungi; KNE63048; KNE63048; AMAG_08214.
DR VEuPathDB; FungiDB:AMAG_08214; -.
DR eggNOG; KOG0450; Eukaryota.
DR OMA; IRIRRHN; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000054350; 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:UP000054350};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 652..862
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1060 AA; 117800 MW; C9047A8371CA94BC CRC64;
MSSRLLQASS TAALAAARTS LRRQAVPALA SASTAGRVLA RKYATANNEA FLAGNAANYV
DEMYAAWRKD PTSVHVSWQA YFANVERGAA PGAAYTAPPS LAPNAGATAA MDSVEVPVLP
TNASSPGEIV DHLKVQLLAR AYQVRGHHLA KLDPLGIHNP ESQGNPPELE PSYYGFSEAD
FDRKFALGPG MLPGYRTSSP QLTLREIVQT LQATYCGTIG IEYAHIPDRG QCDWLRERIE
VPNRVAFSRE DKHMILDRLI WSDSFERFVA TKFPSEKRFG LEGCEALIPG MKALIDRSVD
LGVESIVMGM PHRGRLNVLS NVVRKPNESI FCEFSGTVEP NMAEGSGDVK YHLGMNYDRP
TPSGKRVHLS LVANPSHLEA VNPVVEGKTR AIQFYAGDNE RSKAMPVLLH GDAAFAGQGI
VYETLGFADL PQYATGGTVH IIVNNQIGFT TDPRFSRSTP YCSDVAKTVG APILHVNGDD
VEAVVYACKL AGEWRQKFKK DVVVDIVCYR RHGHNEIDQP MFTQPRMYQI INKQKPVLET
YIEQLLAEGT FTAAEIEAMK QRVWTMLEES YTQSKDYQPT PKDWVSSSWH GFMSPKELAS
LTVAPRDTGL DRDLLRQIGT KVSTIPETFT PHSLIKRIIG QRLKTVEEGE GLDWATAEAI
AFGSLLMERT HLRLSGQDVE RGTFSQRHAV LHDQQTEQTF TALNHLSPDQ AKFTVSNSSL
SEYGVLGFEL GYSLVSPNSL VIWEAQFGDF ANNAQCIIDQ FIASGEKKWL QRTGLVLSLP
HGYDGQGPEH SSSRIERFLQ LCDEDPYKFP TPEELARQHQ DCNMQVCYPS TPANYFHVLR
RQVHRDFRKP LIMPFSKSLL RHPLARSSLA DMGPGTRFQR FLPEVAPESL LPPEDIKTVL
LCSGQVYYAL ARAREVNQIK DVVIGRVEQI SPFPFDKVQQ FVDQYPNAVV RWVQEEPMNM
GPWPFVAPRI QTAMRHSQHH GLVAQRERVE QDPSLVERLT PHGQPLSAPV LYAGRAPSGA
VATGNKKQHL KEERALISEA LFGEIRPVAS VESGVPVYQV
//
