A0PVU7

PR
Gene name
kgd (MUL_4500)
Protein name
Multifunctional 2-oxoglutarate metabolism enzyme
Names
2-hydroxy-3-oxoadipate synthase, HOA synthase, HOAS, 2-oxoglutarate carboxy-lyase, 2-oxoglutarate decarboxylase, Alpha-ketoglutarate decarboxylase, KG decarboxylase, KGD, Alpha-ketoglutarate-glyoxylate carboligase
Species
Mycobacterium ulcerans (strain Agy99)
KEGG Pathway
mul:MUL_4500
EC number
1.2.4.2: With a disulfide as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

14-129 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A0PVU7

Entry ID Method Resolution Chain Position Source
AF-A0PVU7-F1 Predicted AlphaFoldDB

No variants for A0PVU7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A0PVU7

No associated diseases with A0PVU7

5 regional properties for A0PVU7

Type Name Position InterPro Accession
domain Dehydrogenase, E1 component 496 - 824 IPR001017
domain 2-oxoacid dehydrogenase acyltransferase, catalytic domain 109 - 342 IPR001078
domain Transketolase-like, pyrimidine-binding domain 886 - 1086 IPR005475
domain Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal 1091 - 1237 IPR031717
domain 2-oxoglutarate dehydrogenase E1 component, N-terminal domain 5 - 37 IPR032106

Functions

Description
EC Number 1.2.4.2 With a disulfide as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

6 GO annotations of molecular function

Name Definition
2-hydroxy-3-oxoadipate synthase activity Catalysis of the reaction: 2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO(2).
2-oxoglutarate decarboxylase activity Catalysis of the reaction: 2-oxoglutarate + H(+) = CO(2) + succinate semialdehyde.
dihydrolipoyllysine-residue succinyltransferase activity Catalysis of the reaction: succinyl-CoA + dihydrolipoamide = CoA + S-succinyldihydrolipoamide.
magnesium ion binding Binding to a magnesium (Mg) ion.
oxoglutarate dehydrogenase (succinyl-transferring) activity Catalysis of the reaction: 2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO2.
thiamine pyrophosphate binding Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.

1 GO annotations of biological process

Name Definition
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MANISSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY NPESTQEATE PAVVKPAAAP
70 80 90 100 110 120
AKPAPAPAPA KPAAGPPAAG NGSPAAAPSA KPAAAPAKAP APPPAEGDEM QVLRGAAAAV
130 140 150 160 170 180
VKNMSASLDV PTATSVRAVP AKLLIDNRIV INNQLKRNRG GKISFTHLLG YALVQAVKKF
190 200 210 220 230 240
PNMNRHYLDV DGKPNAVTPA HTNLGLAIDL QGKDGKRALV VAGIKRCETM RFAQFVTAYE
250 260 270 280 290 300
DIVRRARDGK LTAEDFSGVT ISLTNPGTIG TVHSVPRLMA GQGAIIGVGA MEYPAEFQGA
310 320 330 340 350 360
SEERIAELGI GKLITLTSTY DHRIIQGAES GDFLRTIHQM LLADEFWDEI FRELSIPYLP
370 380 390 400 410 420
VRWRPDNPDS IVDKNARIIE LIAAYRNRGH LMADIDPLRL DKTRFRSHPD LDVCTHGLTL
430 440 450 460 470 480
WDLDRSFKVG GCFAGPQNMK LRDVLSILRD TYCRHVGVEY THILEPEQQQ WLQQRVEAKH
490 500 510 520 530 540
VKPTVAQQKY VLSKLNAAEA FETFLQTKYV GQKRFSLEGA ESVIPMMDAA IDQCAEYGLD
550 560 570 580 590 600
EVVIGMPHRG RLNVLANIVG KPYSQIFSEF EGNLNPSQAH GSGDVKYHLG ATGVYLQMFG
610 620 630 640 650 660
DNDIQVSLTA NPSHLEAVDP VLEGLVRAKQ DLLEHGETDT ENQRAFSVVP MMLHGDAAFA
670 680 690 700 710 720
GQGVVAETLN LANLPGYRVG GTIHIIVNNQ IGFTTAPEYS RSTEYCTDVA KTIGAPIFHV
730 740 750 760 770 780
NGDDPEACVW VARLAVDFRQ RFNKDVIIDM LCYRRRGHNE GDDPSMTNPR MYDVVDTKRG
790 800 810 820 830 840
VRKSYTEALI GRGDISIKEA EDALRDYQGQ LEQVFNEVRE LEKHGAQPSE SVESDQMIPA
850 860 870 880 890 900
GLATAVDKSL LARIGDAFLA VPDGFTTHPR VQPVLEKRRE MAYEGKIDWA FAELLALGSL
910 920 930 940 950 960
VAEGKLVRFS GQDTRRGTFS QRHSVIIDRH TREEFTPLQL LTTNKDGSPT GGKFLVYDSP
970 980 990 1000 1010 1020
LSEYAAVGFE YGYTVGNPDA VVLWEAQFGD FVNGAQSIID EFISSGEAKW GQLSNVVLLL
1030 1040 1050 1060 1070 1080
PHGHEGQGPD HTSGRIERFL QLWAEGSMTI AMPSTPSNYF HLLRRHALDG IQRPLIVFTP
1090 1100 1110 1120 1130 1140
KSMLRNKAAV SDIKDFTEIK FRSVLEEPTY EDGVGDRNLV NRILLTSGKI YYEMVARKAK
1150 1160 1170 1180 1190 1200
DKREDVAIVR VEQLAPLPRR RLRETLDRYP NAKEFFWVQE EPANQGAWPR FGLELPELLP
1210 1220 1230
EKLSGVKRIS RRAMSAPSSG SSKVHAVEQQ EILDTAFG