ID S2JMC6_MUCC1 Unreviewed; 1032 AA.
AC S2JMC6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=HMPREF1544_03471 {ECO:0000313|EMBL:EPB89672.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB89672.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-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}.
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DR EMBL; KE123931; EPB89672.1; -; Genomic_DNA.
DR AlphaFoldDB; S2JMC6; -.
DR STRING; 1220926.S2JMC6; -.
DR VEuPathDB; FungiDB:HMPREF1544_03471; -.
DR eggNOG; KOG0450; Eukaryota.
DR InParanoid; S2JMC6; -.
DR OMA; IRIRRHN; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000014254; 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:UP000014254};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 651..861
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 977..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 116223 MW; E341C931A8D5220D CRC64;
MYRLSTLSRV TKCVTKQTLL PTTALSYVRP TLTSSYLQAR RHYASPPSVN DGFLHGNAAN
YIEEMYEAWL KDPSSVHLSW QVYFKNMANG VPSGEAYTPP PTIMPSDSAR MPELPTGIAN
MGESSKKVIE HMKIQLLVRA YQVRGHHLAN LDPLHIEHAS TENQHPPELT YQYYGFTDKD
LDRKFTLGPG ILPGMGQTNK ELSLREIIEA LKKMYCGSIG IEYVHIPDRA QCDWIRARVE
KPEPYKYTHD EKKMILDRLT WSDSFERFVA SKYPSEKRFG LEGGETLIPG MKALIDRSVD
LGVESIVIGM PHRGRLNVLS NVVRKPNESI FCEFSGSMEP SDEGSGDVKY HLGMNYVRPT
PSGKRVHLSL VANPSHLEAV DPVVLGKTKA LQFYGKDAHG DHAMSVLMHG DAAMAGQGVV
YETMGFYDLP SYSTGGTIHI VVNNQIGFTT DPRYGRSTPY CTDIAKSINA PVFHVNGDDA
EAVTFVMQLA ADWRQTFHKD CVIDLVCYRK HGHNETDQPM FTQPLMYQAI SKMKPVAQKY
EEQLQKEGEF TAEQIKNEKK RVWEILEESY TASKTYKPSS QEWLSSSWPG FKSPKELATE
ILPQYPTGVS SEVLSQVGKA MTTLPQNFQA HRNISRILQA REKSIASGKD IDWSTAEGLA
WGSLLLENKH VRVSGQDVER GTFSQRHAVL HDQKSDNRAT LLNDISPEQG VLSISNSSLS
EYGVLGFELG YSLVDPNSLV IWEAQFGDFA NTAQVIVDQF LASGEQKWLQ RTGLVLSLPH
GYDGQGPEHS SARIERYLQL CDENPYAFPS AEKLQRQHQD CNMQVVYAST PSQYFHVLRR
QICRDYRKPL ILPFSKSMLR HPLARSNLSE MTGNTHFQLY LPESHPETLV APEQIKKHIL
CSGQVYYALL KAREQNKMND IAISRVEQLN PFPFQQIKEH ADKYPNAEIV WCQEEPLNMG
PWQHVEPRLT TVLAETQHHA GKSPSYAGRP PSASVATGNK KKHYQEEYAF LSKALIGQST
EPRGIEAGVP VW
//
