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CAZyme Information: GBF64323.1

You are here: Home > Sequence: GBF64323.1

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 Trichophyton mentagrophytes
Lineage Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes
CAZyme ID GBF64323.1
CAZy Family GT90
CAZyme Description glutarate-semialdehyde dehydrogenase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1872 BFBS01016373|CGC1 206447.31 7.1286
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TmentagrophytesTIMM2789 7958 N/A 98 7860
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in GBF64323.1.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
188167 SSADH 0.0 68 518 1 448
succinate-semialdehyde dehydrogenase. Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 & G-242, C-293 & G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
223944 AdhE 0.0 50 521 2 466
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion].
395119 Aldedh 0.0 57 520 1 458
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.
215157 PLN02278 0.0 40 526 16 498
succinic semialdehyde dehydrogenase
183050 gabD 0.0 40 523 2 481
NADP-dependent succinate-semialdehyde dehydrogenase I.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.79e-263 531 1313 79 883
3.05e-260 531 1313 79 883
1.25e-258 531 1313 69 874
4.00e-258 531 1373 71 910
1.47e-256 531 1373 22 865

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.41e-175 40 523 1 480
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]
1.96e-175 41 523 2 480
Crystal structure of E. coli NADP dependent enzyme [Escherichia coli]
5.86e-175 41 518 5 478
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]
3.24e-171 41 520 25 498
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]
1.80e-164 52 525 16 487
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.07e-181 40 525 2 483
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
2.44e-179 40 518 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
4.99e-176 41 521 60 543
Putative succinate-semialdehyde dehydrogenase C1002.12c [NADP(+)] OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC1002.12c PE=3 SV=2
2.78e-175 40 523 2 481
Succinate-semialdehyde dehydrogenase [NADP(+)] GabD OS=Escherichia coli (strain K12) OX=83333 GN=gabD PE=1 SV=1
3.29e-172 40 525 3 484
3-sulfolactaldehyde dehydrogenase OS=Pseudomonas putida OX=303 GN=PpSQ1_00395 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000035 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in GBF64323.1.