ID A0A1A9LER7_9FLAO Unreviewed; 923 AA.
AC A0A1A9LER7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=A7A78_10920 {ECO:0000313|EMBL:OAD91760.1};
OS Aequorivita soesokkakensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=1385699 {ECO:0000313|EMBL:OAD91760.1, ECO:0000313|Proteomes:UP000077552};
RN [1] {ECO:0000313|EMBL:OAD91760.1, ECO:0000313|Proteomes:UP000077552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSSK-12 {ECO:0000313|EMBL:OAD91760.1,
RC ECO:0000313|Proteomes:UP000077552};
RA Thevarajoo S., Selvaratnam C., Goh K.M., Chan K.-G., Chong C.S.;
RT "Genome sequencing of Vitellibacter soesokkakensis RSSK-12.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:OAD91760.1}.
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DR EMBL; LXIE01000010; OAD91760.1; -; Genomic_DNA.
DR RefSeq; WP_068761393.1; NZ_LXIE01000010.1.
DR AlphaFoldDB; A0A1A9LER7; -.
DR STRING; 1385699.A7A78_10920; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000077552; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 584..777
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 923 AA; 105442 MW; 3A77DEBE73CE4D28 CRC64;
MDKFSFLNAV HPSYIAELYE KYLQYPDSVE PSWRAFFQGF DFGSENSAHE FFGTNEAVEA
PQYAEGANCE DVVKEFQVVK LIDGYRTRGH LFTKTNPVRE RRKYTPTLAL ENFGLSQHDL
KATFKAGEIL GIGEATLEEI IRHLESIYCD SIGIEYMYIR KPNEIQWIQE KLNINDNQPN
FSTEHKKHIL KKLNEAVAFE SFLHTKYVGQ KRFSLEGGES LIPALDALIE NAAEKGVEEF
VMGMAHRGRL STLTNIFGKS AKDIFSEFDG KDYAQDIFDG DVKYHLGWTS KRKTESGKEI
NLNIAPNPSH LETVGAVVEG ITRAKQDDHH KNNPNKVLPI IVHGDAAIAG QGIVYEIVQM
AQLDGYKTQG TIHIVVNNQI GFTTNYLDAR SSIYCTDVGK VTLSPILHVN ADDVEAVVHA
MLFALDFRME FGRDVFIDLL GYRKYGHNEG DEPRFTQPKL YKAIAKHENP RDIYAEKLIA
QGVIEKGFTD KLEQEYKDKL EESLENSRKE DKTTITPFMQ DEWEGYEYAE EDKMMETVNT
KFDLKKLDEI AEVITKLPED KKFLKKIAKL VEARHTMYFE DNKLDWAMGE LLAYGTLLKE
GHDVRMSGQD VERGTFSHRH AVIKVEDSEE EVVLLNHLKG DQGDFYIYNS LLSEYGVVGF
DYGYSMASPK TLTLWEAQFG DFSNGAQIMI DQYISAAEDK WKLQNGLIML LPHGYEGQGA
EHSSARMERY LQLCANDNMF VADVTTPANL FHLFRRQLKV NYRKPLIVFT PKSLLRHPKV
VSTKEELANG SFQMLIDDAE AKATKVKTLV FVTGKFYYDL LEKREELKRD DVALVRVEQL
FPLPTDAMKK IIKKYKNADD VVWAQEEPKN MGAYSHVLMH FEEARNFRVC SRKMYAAPAA
GSSVRSKARH AKVIENVFDK NMD
//