Q12198
Gene name |
YLL058W (L0569) |
Protein name |
Putative cystathionine gamma-synthase YLL058W |
Names |
O-succinylhomoserine (thiol)-lyase |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YLL058W |
EC number |
2.5.1.47: Transferring alkyl or aryl groups, other than methyl groups |
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 Q12198
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q12198-F1 | Predicted | AlphaFoldDB |
27 variants for Q12198
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s12-23774 | 69 | G>D | No | SGRP | |
| s12-23820 | 84 | K>N | No | SGRP | |
| s12-23826 | 86 | F>L | No | SGRP | |
| s12-23846 | 93 | S>* | No | SGRP | |
| s12-23846 | 93 | S>L | No | SGRP | |
| s12-23845 | 93 | S>T | No | SGRP | |
| s12-23860 | 98 | K>E | No | SGRP | |
| s12-23890 | 108 | I>V | No | SGRP | |
| s12-23900 | 111 | R>H | No | SGRP | |
| s12-23905 | 113 | A>T | No | SGRP | |
| s12-23959 | 131 | A>T | No | SGRP | |
| s12-23981 | 138 | T>I | No | SGRP | |
| s12-24010 | 148 | E>K | No | SGRP | |
| s12-24085 | 173 | L>M | No | SGRP | |
| s12-24110 | 181 | F>S | No | SGRP | |
| s12-24164 | 199 | V>A | No | SGRP | |
| s12-24179 | 204 | R>K | No | SGRP | |
| s12-24188 | 207 | G>D | No | SGRP | |
| s12-24323 | 252 | S>L | No | SGRP | |
| s12-24356 | 263 | Q>P | No | SGRP | |
| s12-24473 | 302 | R>K | No | SGRP | |
| s12-24567 | 333 | M>I | No | SGRP | |
| s12-24591 | 341 | S>R | No | SGRP | |
| s12-24890 | 441 | G>E | No | SGRP | |
| s12-24893 | 442 | I>K | No | SGRP | |
| s12-24926 | 453 | G>E | No | SGRP | |
| s12-24967 | 467 | K>E | No | SGRP |
No associated diseases with Q12198
No regional properties for Q12198
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q12198 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.5.1.47 | Transferring alkyl or aryl groups, other than methyl groups |
| 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 |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| cystathionine gamma-synthase activity | Catalysis of the reaction: O-succinyl-L-homoserine + L-cysteine = cystathionine + succinate. |
| cystathionine gamma-synthase activity (acts on O-phosphohomoserine) | Catalysis of the reaction: L-cysteine + O-phosphonato-L-homoserine = L-cystathionine + hydrogenphosphate. |
| pyridoxal phosphate binding | Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| methionine biosynthetic process | The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. |
| sulfur compound metabolic process | The chemical reactions and pathways involving the nonmetallic element sulfur or compounds that contain sulfur, such as the amino acids methionine and cysteine or the tripeptide glutathione. |
| transsulfuration | The interconversion of homocysteine and cysteine via cystathionine. In contrast with enteric bacteria and mammals, Saccharomyces cerevisiae has two transsulfuration pathways employing two separate sets of enzymes. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTEIEFGQPL | PSNLDYAVSF | GIPTWDSAIG | YAEKVPEVIG | KMATGYPRYF | PQPPVQRLCA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YFVKKFGRGS | ENCRPFPSVN | LGLKCFEYVK | SVSGPESKAH | LEVETVTIKN | RGAKTSKEPA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ELVLTIAAVL | ASEEEFETVK | EYWKLRGECV | SSRLALSVNQ | LLDCANHGSE | QVLRELEAGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FAAKKGEEKA | KNLIKGRIVE | NRFRPFGLEK | KTPNWEGLNL | NPNEDVYLVS | SGMSAISTAR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NLLTFWEEKK | NSGDSLNKTT | SDQKKKPLLC | DTVGIFGFPF | KDTQVIMTKF | GKCKFFGFGN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SRDVVELQKF | LETSKQRILA | VFVETPSNPL | LNMPDLKKLR | SLADQYGFFI | VIDDTIGGLN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VDILPYADIV | STSLTKLFNG | ASNVMGGSVV | LNPKSSLYPY | AREYFRSANF | EDLLWCEDAI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VLERNSRDFE | DRTLRANANT | GILLNDLLLP | EEGKICKKIY | YPTVTSKETF | ENYESVRNER |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GGYGCLFSVA | FFNEGDAKAF | YDSLKVFKGP | SNGTNFTLAC | PYVHLAHHSE | LEEVSKFGAD |
| 550 | 560 | 570 | |||
| PNIIRVSVGL | EDIQWLLKVF | SSALDVVKSR | GSKHS |