You are browsing environment: FUNGIDB
CAZyme Information: PMAA_002480-t26_1-p1
You are here: Home > Sequence: PMAA_002480-t26_1-p1
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Talaromyces marneffei | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei | |||||||||||
| CAZyme ID | PMAA_002480-t26_1-p1 | |||||||||||
| CAZy Family | AA1 | |||||||||||
| CAZyme Description | succinate-semialdehyde dehydrogenase, putative | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | ||||||||||||
Enzyme Prediction help
| EC | 3.2.1.14:2 |
|---|
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH18 | 672 | 1003 | 1.2e-62 | 0.9391891891891891 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 223944 | AdhE | 0.0 | 19 | 490 | 1 | 464 | Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion]. |
| 395119 | Aldedh | 0.0 | 27 | 490 | 1 | 457 | Aldehyde dehydrogenase family. This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity. |
| 143421 | ALDH_F5_SSADH_GabD | 0.0 | 38 | 490 | 1 | 448 | Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like. Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species. |
| 215157 | PLN02278 | 0.0 | 11 | 489 | 17 | 490 | succinic semialdehyde dehydrogenase |
| 143397 | ALDH | 6.53e-178 | 60 | 490 | 2 | 429 | NAD(P)+ dependent aldehyde dehydrogenase family. The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 0.0 | 565 | 1013 | 1 | 448 | |
| 8.14e-207 | 571 | 998 | 7 | 430 | |
| 5.67e-90 | 627 | 998 | 81 | 453 | |
| 1.68e-87 | 615 | 1000 | 27 | 427 | |
| 7.12e-86 | 627 | 1001 | 113 | 490 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7.49e-130 | 8 | 495 | 2 | 484 | Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_2 Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_3 Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_4 Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_5 Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_6 Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_A Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_B Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_C Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_D Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_E Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_F Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_G Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_H Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_I Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_J Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_K Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_L Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_M Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_N Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_O Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_P Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_Q Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_R Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_S Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_T Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_U Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_V Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_W Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_X Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_Y Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],4V6H_Z Crystal structure of succinate-semialdehyde dehydrogenase from Burkholderia pseudomallei [Burkholderia pseudomallei 1710b] |
|
| 2.81e-129 | 11 | 489 | 25 | 496 | Crystal structure of aldehyde dehydrogenase from brucella melitensis biovar abortus 2308 [Brucella abortus 2308],3EK1_B Crystal structure of aldehyde dehydrogenase from brucella melitensis biovar abortus 2308 [Brucella abortus 2308],3EK1_C Crystal structure of aldehyde dehydrogenase from brucella melitensis biovar abortus 2308 [Brucella abortus 2308],3EK1_D Crystal structure of aldehyde dehydrogenase from brucella melitensis biovar abortus 2308 [Brucella abortus 2308],3EK1_E Crystal structure of aldehyde dehydrogenase from brucella melitensis biovar abortus 2308 [Brucella abortus 2308],3EK1_F Crystal structure of aldehyde dehydrogenase from brucella melitensis biovar abortus 2308 [Brucella abortus 2308],3EK1_G Crystal structure of aldehyde dehydrogenase from brucella melitensis biovar abortus 2308 [Brucella abortus 2308],3EK1_H Crystal structure of aldehyde dehydrogenase from brucella melitensis biovar abortus 2308 [Brucella abortus 2308] |
|
| 1.02e-126 | 16 | 489 | 10 | 480 | The crystal structure of the oxidized form of human SSADH [Homo sapiens],2W8O_A The crystal structure of the reduced form of human SSADH [Homo sapiens] |
|
| 2.14e-125 | 16 | 489 | 10 | 480 | The crystal structure of human C340A SSADH [Homo sapiens],2W8Q_A The crystal structure of human SSADH in complex with SSA. [Homo sapiens],2W8R_A The crystal structure of human SSADH in complex with NAD+ [Homo sapiens] |
|
| 9.57e-125 | 10 | 489 | 1 | 475 | Crystal structure of E. coli NADP dependent enzyme [Escherichia coli],3JZ4_B Crystal structure of E. coli NADP dependent enzyme [Escherichia coli],3JZ4_D Crystal structure of E. coli NADP dependent enzyme [Escherichia coli] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.19e-132 | 10 | 489 | 3 | 477 | 3-sulfolactaldehyde dehydrogenase OS=Pseudomonas putida OX=303 GN=PpSQ1_00395 PE=1 SV=1 |
|
| 1.55e-127 | 10 | 489 | 2 | 476 | Glutarate-semialdehyde dehydrogenase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=davD PE=1 SV=1 |
|
| 8.38e-127 | 21 | 490 | 75 | 541 | Putative succinate-semialdehyde dehydrogenase C1002.12c [NADP(+)] OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC1002.12c PE=3 SV=2 |
|
| 1.08e-126 | 10 | 489 | 2 | 474 | Glutarate-semialdehyde dehydrogenase OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=davD PE=3 SV=1 |
|
| 1.16e-126 | 1 | 489 | 1 | 486 | Putative succinate-semialdehyde dehydrogenase C139.05 [NADP(+)] OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC139.05 PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000053 | 0.000000 |
