Search Results

Overview

Uniprot IDQ96HY7
Protein Name2-oxoadipate dehydrogenase complex component E1
Gene NameDHTKD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
553 QMHSHLLKTHVQSRM
818 KHFYSLVKQRESLGA
827 RESLGAKKHDFAIIR

Function

2-oxoadipate dehydrogenase (E1a) component of the 2-oxoadipate dehydrogenase complex (OADHC) (PubMed:29191460, PubMed:29752936, PubMed:32303640, PubMed:32633484, PubMed:32695416). Participates in the first step, rate limiting for the overall conversion of 2-oxoadipate (alpha-ketoadipate) to glutaryl-CoA and CO(2) catalyzed by the whole OADHC (PubMed:29191460, PubMed:32695416). Catalyzes the irreversible decarboxylation of 2-oxoadipate via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST) (Probable) (PubMed:29752936, PubMed:32303640, PubMed:32633484). Can catalyze the decarboxylation of 2-oxoglutarate in vitro, but at a much lower rate than 2-oxoadipate (PubMed:29191460, PubMed:29752936, PubMed:32633484, PubMed:32695416). Responsible for the last step of L-lysine, L-hydroxylysine and L-tryptophan catabolism with the common product being 2-oxoadipate (Probable)

Protein Sequence

10 MASATAAAAR 20 RGLGRALPLF 30 WRGYQTERGV 40 YGYRPRKPES 50 REPQGALERP 60 PVDHGLARLV 70 TVYCEHGHKA 80 AKINPLFTGQ 90 ALLENVPEIQ 100 ALVQTLQGPF 110 HTAGLLNMGK 120 EEASLEEVLV 130 YLNQIYCGQI 140 SIETSQLQSQ 150 DEKDWFAKRF 160 EELQKETFTT 170 EERKHLSKLM 180 LESQEFDHFL 190 ATKFSTVKRY 200 GGEGAESMMG 210 FFHELLKMSA 220 YSGITDVIIG 230 MPHRGRLNLL 240 TGLLQFPPEL 250 MFRKMRGLSE 260 FPENFSATGD 270 VLSHLTSSVD 280 LYFGAHHPLH 290 VTMLPNPSHL 300 EAVNPVAVGK 310 TRGRQQSRQD 320 GDYSPDNSAQ 330 PGDRVICLQV 340 HGDASFCGQG 350 IVPETFTLSN 360 LPHFRIGGSV 370 HLIVNNQLGY 380 TTPAERGRSS 390 LYCSDIGKLV 400 GCAIIHVNGD 410 SPEEVVRATR 420 LAFEYQRQFR 430 KDVIIDLLCY 440 RQWGHNELDE 450 PFYTNPIMYK 460 IIRARKSIPD 470 TYAEHLIAGG 480 LMTQEEVSEI 490 KSSYYAKLND 500 HLNNMAHYRP 510 PALNLQAHWQ 520 GLAQPEAQIT 530 TWSTGVPLDL 540 LRFVGMKSVE 550 VPRELQMHSH 560 LLKTHVQSRM 570 EKMMDGIKLD 580 WATAEALALG 590 SLLAQGFNVR 600 LSGQDVGRGT 610 FSQRHAIVVC 620 QETDDTYIPL 630 NHMDPNQKGF 640 LEVSNSPLSE 650 EAVLGFEYGM 660 SIESPKLLPL 670 WEAQFGDFFN 680 GAQIIFDTFI 690 SGGEAKWLLQ 700 SGIVILLPHG 710 YDGAGPDHSS 720 CRIERFLQMC 730 DSAEEGVDGD 740 TVNMFVVHPT 750 TPAQYFHLLR 760 RQMVRNFRKP 770 LIVASPKMLL 780 RLPAAVSTLQ 790 EMAPGTTFNP 800 VIGDSSVDPK 810 KVKTLVFCSG 820 KHFYSLVKQR 830 ESLGAKKHDF 840 AIIRVEELCP 850 FPLDSLQQEM 860 SKYKHVKDHI 870 WSQEEPQNMG 880 PWSFVSPRFE 890 KQLACKLRLV 900 GRPPLPVPAV 910 GIGTVHLHQH EDILAKTFA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0160167 oxoadipate dehydrogenase complex
Molecular Function GO:0160166 2-oxoadipate dehydrogenase activity
Molecular Function GO:0030976 thiamine pyrophosphate binding
Biological Process GO:0006091 generation of precursor metabolites and energy
Biological Process GO:0006096 glycolytic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.