A1TDK2

PR
Gene name
kgd (Mvan_4477)
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
Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii)
KEGG Pathway
mva:Mvan_4477
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)

5-142 (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 A1TDK2

Entry ID Method Resolution Chain Position Source
AF-A1TDK2-F1 Predicted AlphaFoldDB

No variants for A1TDK2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1TDK2

No associated diseases with A1TDK2

5 regional properties for A1TDK2

Type Name Position InterPro Accession
domain Dehydrogenase, E1 component 505 - 829 IPR001017
domain 2-oxoacid dehydrogenase acyltransferase, catalytic domain 117 - 352 IPR001078
domain Transketolase-like, pyrimidine-binding domain 891 - 1091 IPR005475
domain Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal 1096 - 1242 IPR031717
domain 2-oxoglutarate dehydrogenase E1 component, N-terminal domain 6 - 36 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
MNSPSPFGQN EWLVEEMYRK FREDPSSVDP SWHEFLVDYS PEPTNDAPAG NGKPAAAPTA
70 80 90 100 110 120
PPEPASAPAP KPASTNGGAP PAKADTSTTR APEKKPEEKT SPAPKAKTAA PAGVSDDDET
130 140 150 160 170 180
QVLRGAAAAV VKNMSASLDV PTATSVRAIP AKAMIDNRIV INNHLKRTRG GKISFTHLLG
190 200 210 220 230 240
YAIVQAVKKF PNMNRHFAEI DGKPVAVTPA HTNLGLAIDL PGKDGKRSLV VAAIKNCETM
250 260 270 280 290 300
HFGQFIAAYE DIVRRARDGK LTAEDFAGVT ISLTNPGTIG TVHSVPRLMK GQGAIVGAGA
310 320 330 340 350 360
MEYPAEFQGA SEERIAELGV GKLMTLTSTY DHRIIQGAES GDFLRTIHTL LLDDEFYDEI
370 380 390 400 410 420
FRELGIPHEP VRWRIDNPDS IEDKNARVIE LIAAYRNRGH LMADIDPLRL DKTRFRSHPD
430 440 450 460 470 480
LDVNTHGLTL WDLDREFKVN GFAGKTHKKL RDILGLLRDA YCRHIGVEYT HILEPEQQQW
490 500 510 520 530 540
LQERIEVKHE KPTVAEQKYI LSKLNAAEAF ETFLQTKYVG QKRFSLEGAE TVIPMMDAAI
550 560 570 580 590 600
DQCAEHGLDE VVIGMPHRGR LNVLANIVGK PYSQIFTEFE GNLNPSQAHG SGDVKYHLGA
610 620 630 640 650 660
NGTYIQMFGD NDIDVSLVAN PSHLEAVDPV LEGLVRAKQD ILDKGNGPDG FTVVPMMLHG
670 680 690 700 710 720
DAAFAGQGVV AETLNLALLR GYRTGGTIHI IVNNQIGFTT SPYDSRSSEY CTDVAKMIGA
730 740 750 760 770 780
PIFHVNGDDP EACVWVAKLA VDFRQKFKKD VVIDMLCYRR RGHNEGDDPS MTQPTMYDVI
790 800 810 820 830 840
DTKRGVRKSY TEALIGRGDI SMKEAEDALR DYQGQLERVF NEVRELEKHA IAPSSSVESD
850 860 870 880 890 900
QMVPAGMSTA VDKSLLARIG DAHLGYPDDF NVHPRVKPVL EKRREMAYEG KVDWAFAELL
910 920 930 940 950 960
ALGTFLAEGK TIRFTGQDTR RGTFTQRHSV IIDRQTGREF TPLDLLTVDS DGNPTGGKFM
970 980 990 1000 1010 1020
AYDSALSEFA AVGFEYGYSV GNPNALVLWE AQFGDFVNGA QSIIDEFISS GEAKWGQLSD
1030 1040 1050 1060 1070 1080
VVLLLPHGHE GQGPDHTSGR IERFLLLWAE GSMTIAMPST PANYFHLLRR HGLDGIHRPL
1090 1100 1110 1120 1130 1140
IVFTPKSMLR NKAAVSDLKD FTEMKFRSVL EEPTYTEGTG DRSKAKRILL TSGKLYYELA
1150 1160 1170 1180 1190 1200
ARKSKEGRDD VAILRLEQLA PLPKRRLAAT LDEYPNAEQY FWVQEEPANQ GAWPTLGLTL
1210 1220 1230 1240
PEVLPEKLAG IKRISRRAMS APSSGSSKVH AVEQQEIIDE AFG