Basic Information

NameSuccinate-semialdehyde dehydrogenase [NADP(+)] (SSDH) (EC 1.2.1.16)
Uniprot IDP38067
Systematic gene nameYBR006W
Standard gene nameUGA2
Gene namesUGA2 UGA5 YBR006W YBR0112
Description from SGDYBR006W UGA2 SGDID:S000000210, Chr II from 247010-248503, Genome Release 64-3-1, Verified ORF, "Succinate semialdehyde dehydrogenase; involved in the utilization of gamma-aminobutyrate (GABA) as a nitrogen source; part of the 4-aminobutyrate and glutamate degradation pathways; localized to the cytoplasm"
Protein length497
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MTLSKYSKPT LNDPNLFRES GYIDGKWVKG TDEVFEVVDP ASGEIIARVP
EQPVSVVEEA IDVAYETFKT YKNTTPRERA KWLRNMYNLM LENLDDLATI
ITLENGKALG EAKGEIKYAA SYFEWYAEEA PRLYGATIQP LNPHNRVFTI
RQPVGVCGII CPWNFPSAMI TRKAAAALAV GCTVVIKPDS QTPLSALAMA
YLAEKAGFPK GSFNVILSHA NTPKLGKTLC ESPKVKKVTF TGSTNVGKIL
MKQSSSTLKK LSFELGGNAP FIVFEDADLD QALEQAMACK FRGLGQTCVC
ANRLYVHSSI IDKFAKLLAE RVKKFVIGHG LDPKTTHGCV INSSAIEKVE
RHKQDAIDKG AKVVLEGGRL TELGPNFYAP VILSHVPSTA IVSKEETFGP
LCPIFSFDTM EEVVGYANDT EFGLAAYVFS KNVNTLYTVS EALETGMVSC
NTGVFSDCSI PFGGVKESGF GREGSLYGIE DYTVLKTITI GNLPNSI

Legend

  • X Phoshorylation
  • X K-acetylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


Use imported representation

Loading structure from server... It may take a while.

If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.

References

[137, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[232, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[313, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[316, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[475, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[475, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[475, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[496, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)