ID S9VV21_9TRYP Unreviewed; 707 AA.
AC S9VV21;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN ORFNames=STCU_03672 {ECO:0000313|EMBL:EPY31031.1}, STCU_09117
GN {ECO:0000313|EMBL:EPY20190.1};
OS Strigomonas culicis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY31031.1, ECO:0000313|Proteomes:UP000015354};
RN [1] {ECO:0000313|EMBL:EPY31031.1, ECO:0000313|Proteomes:UP000015354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23560078;
RA Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA de Souza W., Schenkman S., de Vasconcelos A.T.;
RT "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT Family.";
RL PLoS ONE 8:E60209-E60209(2013).
RN [2] {ECO:0000313|EMBL:EPY31031.1}
RP NUCLEOTIDE SEQUENCE.
RA Motta M.C.M., Martins A.C.A., Preta C.M.C.C., Silva R., de Souza S.S.,
RA Klein C.C., de Almeida L.G.P., Cunha O.L., Colabardini A.C., Lima B.A.,
RA Machado C.R., Soares C.M.A., de Menezes C.B.A., Bartolomeu D.C.,
RA Grisard E.C., Fantinatti-Garboggini F., Rodrigues-Luiz G.F., Wagner G.,
RA Goldman G.H., Fietto J.L.R., Ciapina L.P., Brocchi M., Elias M.C.,
RA Goldman M.H.S., Sagot M.-F., Pereira M., Stoco P.H., Teixeira S.M.R.,
RA de Mendonca-Neto R.P., Maciel T.E.F., Mendes T.A.O., Urmenyi T.P.,
RA Teixeira M.M.G., de Camargo E.F.P., de Sousa W., Schenkman S.,
RA de Vasconcelos A.T.R.;
RL Submitted (MAR-2013) 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}.
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:EPY31031.1}.
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DR EMBL; ATMH01009117; EPY20190.1; -; Genomic_DNA.
DR EMBL; ATMH01003672; EPY31031.1; -; Genomic_DNA.
DR AlphaFoldDB; S9VV21; -.
DR EnsemblProtists; EPY20190; EPY20190; STCU_09117.
DR EnsemblProtists; EPY31031; EPY31031; STCU_03672.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000015354; 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; 3.40.50.970; -; 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; IPR029061; THDP-binding.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000015354};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 33..70
FT /note="2-oxoglutarate dehydrogenase E1 component N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16078"
FT DOMAIN 233..531
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 530..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 79331 MW; 98FB10E791936889 CRC64;
MMRRMLSGAV FAQHGIRAYT DAKTIRKPNP YDQILQSSNQ EYVEHLLAKY EEDRALVDPS
WIPIFDAMRS RDFDQPIVLT FSRPYDPKSI SEKQRLDNMR LAWMIREYEE SGHYFADTNP
LKGILEPDHS IDSNLLDPLT FGFSPDDLKQ VFNVTFGANH EATFVSGGTA MTLEQIIDKM
HRMYCGPIGF EFMSSGFFDV RNWFRQEILY SLQPLSIPNK KLIYNDVVKA CGLEKFLQIK
YATQQRFGLD GGEATIPALN AILMEAASSG MDSAIIGMAH RGRLNTLANV CHMSIHSILN
EFEGNVPEHL RDLNGDVKYH IGINHGLKLP DGQHINIEMI PNPSHLEAVN PLVLGKVRAR
QAMRNDVECT SVLPLLIHGD ASFTGQGSCY ETMGFCELEN FHCGGTVHVV INNQIGFTTS
PDQGRATRYC TDLAKVNNAP VMHVNGHNVE ACVKAARIAA RFRQQFHRDI ILDIVCYRRN
GHNEQDLPDF TQPQMYDYIR KLPPLVDIYS KQLIEEGVIL ADERATKEKE WEGNHAPRVR
PPQQCPRLRE GGACVRPRVG EHVRGARRAQ VGEAKARRAQ AEADRDRCER PGAAAGRHAH
HVHPEGDAGG APRRAAHVRG APEGHRERRR RGVVPGGAAR LRHALAAGRP HPPHRRGRGA
WHLHAAPRRH HGPEDEPQVL PRADPLALAG AHHHLEQLAV GARLLRV
//