Q73WX4
Gene name |
kgd (MAP_2536) |
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 paratuberculosis (strain ATCC BAA-968 / K-10) (Mycobacterium paratuberculosis) |
KEGG Pathway |
mpa:MAP_2536 |
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)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q73WX4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q73WX4-F1 | Predicted | AlphaFoldDB |
No variants for Q73WX4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q73WX4 | |||||
No associated diseases with Q73WX4
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 |
| MSNISSPFGQ | NEWLVEEMYR | KFRDDPSSVD | PSWHEFLVDY | NPEPTGDSVL | AAPASTDGPS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| APAPAAPQTA | QPALPAQTAP | PAQTAQPARP | APQPAAAPGN | GASTRPAKPA | TPPPAEGDEL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QTLRGAAAAV | VKNMSASLEV | PTATSVRAIP | AKLLIDNRIV | INNQLKRTRG | GKISFTHLLG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YALVQAIKKF | PNMNRHYAEI | DGKPTAITPA | HTNLGLAIDL | QGKDGKRSLV | VAGIKNCETM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RFAQFVTAYE | DIVRRARDGK | LTAEDFAGVT | ISLTNPGTIG | TVHSVPRLMN | GQGAIIGVGA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MEYPAEFQGA | SEERIAELGI | GKLITLTSTY | DHRIIQGAES | GDFLRTIHEM | LLSDGFWDDI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FRELSIPYLP | IRWSTDNPDS | IVDKNARVME | LIAAYRNRGH | LMADIDPLRL | DGSRFRSHPD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LEILNHGLTL | WDLDRVFKVN | GFAGAEYKKL | RDILGLLRDA | YCRHIGVEYT | HILDPEQQEW |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LQQRVETKHV | KPTVAEQKFI | LSKLNAAEAF | ETFLQTKYVG | QKRFSLEGAE | SVIPMMDAAI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DQCAEHGLDE | VVIGMPHRGR | LNVLANIVGK | PYSQIFSEFE | GNLNPAQAHG | SGDVKYHLGA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| TGVYLQMFGD | NDIQVSLTAN | PSHLEAVDPV | LEGLVRAKQD | LLDHGADDQG | DEKAFSVVPM |
| 670 | 680 | 690 | 700 | 710 | 720 |
| MLHGDAAFAG | QGVVAETLNL | THLPGYRVGG | TIHIIVNNQI | GFTTAPEHSR | SSEYCTDVAK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| MIGAPIFHVN | GDDPEACAWV | AKLAVDFRQK | FKKDVVIDML | CYRKRGHNEG | DDPSMTNPAM |
| 790 | 800 | 810 | 820 | 830 | 840 |
| YDVVDIKRGV | RKSYTEALIG | RGDISMKEAE | DALRDYQGQL | ERVFNEVREL | EKHGVGPSES |
| 850 | 860 | 870 | 880 | 890 | 900 |
| VEADQMLPAG | LATAVDKALL | ARIGDAFLAL | PEGFTAHPRV | QPVLEKRREM | AYEGKIDWAF |
| 910 | 920 | 930 | 940 | 950 | 960 |
| AELLALGSLV | AGGKLVRLSG | QDTRRGTFSQ | RHSVIIDRNT | GEEFTPLQLL | ATNPDGTPTG |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| GKFLVYDSPL | SEYAAVGFEY | GYTVGNPDAL | VLWEAQFGDF | VNGAQSIIDE | FISSGEAKWG |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| QLSNVVLLLP | HGHEGQGPDH | TSARIERFLQ | LWAEGSMTIA | MPSTPSNYFH | LLRRHALDGI |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| KRPLIVFTPK | SMLRNKAAVS | DIKDFTEIKF | RSVLEEPTYE | DGIGDRGKVS | RVLLTSGKLY |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| YELVARKNKD | NRDDVAIVRI | EQLAPLPKRR | LGETLDRYPN | VREYFWVQEE | PANQGAWPRF |
| 1210 | 1220 | 1230 | 1240 | ||
| GLELPELLPD | KLTGLKRISR | RAMSAPSSGS | SKVHAVEQQE | IIDTAFA |