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Database: UniProt
Entry: S9VV21_9TRYP
LinkDB: S9VV21_9TRYP
Original site: S9VV21_9TRYP 
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
//
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