ID A0A0F4RLI5_9RHOB Unreviewed; 985 AA.
AC A0A0F4RLI5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN Name=sucA {ECO:0000313|EMBL:KJZ20846.1};
GN ORFNames=TW80_08915 {ECO:0000313|EMBL:KJZ20846.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ20846.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ20846.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ20846.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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:KJZ20846.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXYE01000002; KJZ20846.1; -; Genomic_DNA.
DR RefSeq; WP_045996864.1; NZ_JXYE01000002.1.
DR AlphaFoldDB; A0A0F4RLI5; -.
DR STRING; 579483.TW80_08915; -.
DR PATRIC; fig|579483.3.peg.1826; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000033741; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KJZ20846.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033741};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 628..821
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 57..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 109820 MW; C8F4DDFE9C6B4947 CRC64;
MNDQSPNDIF HASSFLQGHN AEYVEQLYAR YADNPNTVDE SWQEFFKALG DAPAEAKAEA
AGPSWSRLDW PQTPNDDLTA ALDGQWPAEP AAAGKKIKDK AAEKGVSLSE DQIRAAVLDS
VRALMIIRAY RIRGHLIADL DPLGMRSNEP HPELDPASYG FTAADMDRPI FIDNVLGLEV
ATMNEIIAIV KRTYCGTFAL QYMHISNPEE AGWLKERIEG YGKEIAFTKE GRKAILNSLV
EAEGFEKFLH VKYMGTKRFG LDGGESLIPA MEQIIKRGGQ LGLEDIVIGM PHRGRLSVLA
NVMEKPYRAI FNEFQGGSFK PEDVDGSGDV KYHLGASSDR AFDGNNVHLS LTANPSHLEA
VNPVVLGKVR AKQDQLGDTD RTKVMGVLLH GDAAFAGQGV VAEGFGLSGL RGHRTGGTMH
IVVNNQIGFT TAPHFSRSSP YPTDIALMVE APIFHVNGDD PEAVVHAARV ATEFRQKFHK
DVVLDIICYR RFGHNEGDEP MFTNPMMYKK IKKQKTTLTL YTERLVKDGL IPEGEIEDMK
ASFQAHLNAE FETGKTYKPN KADWLDGKWS HLDTQKEDYQ RGATAIDEKT FAEVGRALTN
VPEGFPLHKT VGRILKAKEQ MFETGEGIDW ATGEALAFGS LMTEGYPVRL SGQDSTRGTF
SQRHSGLINQ ENEDRFYPLN HIREGQAHYE VIDSMLSEYA VLGFEYGYSL AEPNALTLWE
AQFGDFANGA QIMFDQFISS GESKWLRMSG LVCLLPHGYE GQGPEHSSAR LERFLTMCGG
DNWIVANCTT PANYFHILRR QLHRSYRKPL IMMTPKSLLR HKLAVSKAEE FTTGSSFHRV
LWDDAQQGNS DTKLVADDKI KRVVMCSGKV YYDLLEERDK RGLNDVYILR FEQFYPFPAQ
SAVNELERFK NAEMVWCQEE PKNQGAWSFI EPNIEWVLTR IGAKHSRPVY AGRAASASPA
TGLASKHKAE QTALVNDALT IEGTK
//
