A1KI36

PR
Gene name
kgd (BCG_1308c)
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 bovis (strain BCG / Pasteur 1173P2)
KEGG Pathway
mbb:BCG_1308c
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)

28-109 (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 A1KI36

Entry ID Method Resolution Chain Position Source
AF-A1KI36-F1 Predicted AlphaFoldDB

No variants for A1KI36

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1KI36

No associated diseases with A1KI36

5 regional properties for A1KI36

Type Name Position InterPro Accession
domain Dehydrogenase, E1 component 489 - 817 IPR001017
domain 2-oxoacid dehydrogenase acyltransferase, catalytic domain 103 - 335 IPR001078
domain Transketolase-like, pyrimidine-binding domain 879 - 1080 IPR005475
domain Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal 1084 - 1230 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 NEWLVEAMYR KFRDDPSSVD PSWHEFLVDY SPEPTSQPAA EPTRVTSPLV
70 80 90 100 110 120
AERAAAAAPQ APPKPADTAA AGNGVVAALA AKTAVPPPAE GDEVAVLRGA AAAVVKNMSA
130 140 150 160 170 180
SLEVPTATSV RAVPAKLLID NRIVINNQLK RTRGGKISFT HLLGYALVQA VKKFPNMNRH
190 200 210 220 230 240
YTEVDGKPTA VTPAHTNLGL AIDLQGKDGK RSLVVAGIKR CETMRFAQFV TAYEDIVRRA
250 260 270 280 290 300
RDGKLTTEDF AGVTISLTNP GTIGTVHSVP RLMPGQGAII GVGAMEYPAE FQGASEERIA
310 320 330 340 350 360
ELGIGKLITL TSTYDHRIIQ GAESGDFLRT IHELLLSDGF WDEVFRELSI PYLPVRWSTD
370 380 390 400 410 420
NPDSIVDKNA RVMNLIAAYR NRGHLMADTD PLRLDKARFR SHPDLEVLTH GLTLWDLDRV
430 440 450 460 470 480
FKVDGFAGAQ YKKLRDVLGL LRDAYCRHIG VEYAHILDPE QKEWLEQRVE TKHVKPTVAQ
490 500 510 520 530 540
QKYILSKLNA AEAFETFLQT KYVGQKRFSL EGAESVIPMM DAAIDQCAEH GLDEVVIGMP
550 560 570 580 590 600
HRGRLNVLAN IVGKPYSQIF TEFEGNLNPS QAHGSGDVKY HLGATGLYLQ MFGDNDIQVS
610 620 630 640 650 660
LTANPSHLEA VDPVLEGLVR AKQDLLDHGS IDSDGQRAFS VVPLMLHGDA AFAGQGVVAE
670 680 690 700 710 720
TLNLANLPGY RVGGTIHIIV NNQIGFTTAP EYSRSSEYCT DVAKMIGAPI FHVNGDDPEA
730 740 750 760 770 780
CVWVARLAVD FRQRFKKDVV IDMLCYRRRG HNEGDDPSMT NPYMYDVVDT KRGARKSYTE
790 800 810 820 830 840
ALIGRGDISM KEAEDALRDY QGQLERVFNE VRELEKHGVQ PSESVESDQM IPAGLATAVD
850 860 870 880 890 900
KSLLARIGDA FLALPNGFTA HPRVQPVLEK RREMAYEGKI DWAFGELLAL GSLVAEGKLV
910 920 930 940 950 960
RLSGQDSRRG TFSQRHSVLI DRHTGEEFTP LQLLATNSDG SPTGGKFLVY DSPLSEYAAV
970 980 990 1000 1010 1020
GFEYGYTVGN PDAVVLWEAQ FGDFVNGAQS IIDEFISSGE AKWGQLSNVV LLLPHGHEGQ
1030 1040 1050 1060 1070 1080
GPDHTSARIE RFLQLWAEGS MTIAMPSTPS NYFHLLRRHA LDGIQRPLIV FTPKSMLRHK
1090 1100 1110 1120 1130 1140
AAVSEIKDFT EIKFRSVLEE PTYEDGIGDR NKVSRILLTS GKLYYELAAR KAKDNRNDLA
1150 1160 1170 1180 1190 1200
IVRLEQLAPL PRRRLRETLD RYENVKEFFW VQEEPANQGA WPRFGLELPE LLPDKLAGIK
1210 1220 1230
RISRRAMSAP SSGSSKVHAV EQQEILDEAF G