Q91WT9
SS
Gene name |
Cbs |
Protein name |
Cystathionine beta-synthase |
Names |
EC 4.2.1.22 , Beta-thionase , Serine sulfhydrase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:12411 |
EC number |
4.2.1.22: Hydro-lyases |
Protein Class |
|
Descriptions
Cystathionine beta-synthase (CBS) is a key regulatory point in the biosynthesis of cysteine via the transsulfuration pathway. CBS is activated by S-adenosyl-L-methionine (AdoMet) by inducing a conformational change involving a noncatalytic C-terminal region spanning residues 414-551. The discovery of mutants (S466L and I435T) from patients represents the autoinhibitory role of the C-terminal region.
Autoinhibitory domains (AIDs)
Target domain |
35-409 (Catalytic domain) |
Relief mechanism |
Ligand binding, Cleavage, Others |
Assay |
|
Accessory elements
No accessory elements
References
- Janosík M et al. (2001) "Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region", Biochemistry, 40, 10625-33
- Ereño-Orbea J et al. (2014) "Structural insight into the molecular mechanism of allosteric activation of human cystathionine β-synthase by S-adenosylmethionine", Proceedings of the National Academy of Sciences of the United States of America, 111, E3845-52
Autoinhibited structure
Activated structure
1 structures for Q91WT9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q91WT9-F1 | Predicted | AlphaFoldDB |
31 variants for Q91WT9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs235480183 | 15 | G>V | No | EVA | |
| rs48180803 | 58 | A>V | No | EVA | |
| rs13482947 | 59 | D>E | No | EVA | |
| rs3389449494 | 59 | D>N | No | EVA | |
| rs3389430316 | 123 | M>I | No | EVA | |
| rs3389420090 | 131 | G>E | No | EVA | |
| rs3389449427 | 139 | I>L | No | EVA | |
| rs3389409964 | 145 | G>S | No | EVA | |
| rs3389461297 | 187 | R>T | No | EVA | |
| rs3389461292 | 189 | P>L | No | EVA | |
| rs3389452842 | 256 | G>C | No | EVA | |
| rs3407925796 | 273 | K>GGQL* | No | EVA | |
| rs3406586663 | 274 | I>V | No | EVA | |
| rs241567272 | 288 | E>K | No | EVA | |
| rs3389449465 | 338 | Q>* | No | EVA | |
| rs260765752 | 359 | R>P | No | EVA | |
| rs260765752 | 359 | R>Q | No | EVA | |
| rs3389430340 | 369 | V>I | No | EVA | |
| rs3389442045 | 377 | N>I | No | EVA | |
| rs3389363704 | 386 | K>E | No | EVA | |
| rs29501189 | 407 | R>H | No | EVA | |
| rs265346779 | 429 | D>G | No | EVA | |
| rs3389449444 | 450 | A>P | No | EVA | |
| rs3389445327 | 450 | A>V | No | EVA | |
| rs3389449448 | 451 | I>V | No | EVA | |
| rs245524886 | 477 | K>R | No | EVA | |
| rs3389450300 | 484 | K>E | No | EVA | |
| rs262274481 | 501 | M>I | No | EVA | |
| rs3389458654 | 521 | G>E | No | EVA | |
| rs3389466944 | 526 | P>S | No | EVA | |
| rs3389466951 | 545 | T>N | No | EVA |
No associated diseases with Q91WT9
5 regional properties for Q91WT9
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.1.22 | Hydro-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
14 GO annotations of molecular function
| Name | Definition |
|---|---|
| carbon monoxide binding | Binding to carbon monoxide (CO). |
| cystathionine beta-synthase activity | Catalysis of the reaction |
| cysteine synthase activity | Catalysis of the reaction |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| L-cysteine desulfhydrase activity | Catalysis of the reaction |
| metal ion binding | Binding to a metal ion. |
| modified amino acid binding | Binding to a modified amino acid. |
| nitric oxide binding | Binding to nitric oxide (NO). |
| nitrite reductase (NO-forming) activity | Catalysis of the reaction |
| oxygen binding | Binding to oxygen (O2). |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| 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. |
| S-adenosyl-L-methionine binding | Binding to S-adenosyl-L-methionine. |
| ubiquitin protein ligase binding | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. |
22 GO annotations of biological process
| Name | Definition |
|---|---|
| blood vessel diameter maintenance | Any process that modulates the diameter of blood vessels. |
| blood vessel remodeling | The reorganization or renovation of existing blood vessels. |
| cartilage development involved in endochondral bone morphogenesis | The process whose specific outcome is the progression of the cartilage that will provide a scaffold for mineralization of endochondral bones. |
| cellular response to hypoxia | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. |
| cerebellum morphogenesis | The process in which the anatomical structure of the cerebellum is generated and organized. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills. |
| cysteine biosynthetic process | The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid. |
| cysteine biosynthetic process from serine | The chemical reactions and pathways resulting in the formation of cysteine from other compounds, including serine. |
| cysteine biosynthetic process via cystathionine | The chemical reactions and pathways resulting in the formation of cysteine, via the intermediate cystathionine. |
| DNA protection | Any process in which DNA is protected from damage by, for example, oxidative stress. |
| endochondral ossification | Replacement ossification wherein bone tissue replaces cartilage. |
| homocysteine catabolic process | The chemical reactions and pathways resulting in the breakdown of homocysteine, the amino acid alpha-amino-gamma-mercaptobutanoic acid. |
| homocysteine metabolic process | The chemical reactions and pathways involving homocysteine, the amino acid alpha-amino-gamma-mercaptobutanoic acid. Homocysteine is an important intermediate in the metabolic reactions of its S-methyl derivative, methionine. |
| hydrogen sulfide biosynthetic process | The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S. |
| L-cysteine catabolic process | The chemical reactions and pathways resulting in the breakdown of L-cysteine, the L-enantiomer of 2-amino-3-mercaptopropanoic acid, i.e. (2R)-2-amino-3-mercaptopropanoic acid. |
| L-serine catabolic process | The chemical reactions and pathways resulting in the breakdown of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid. |
| L-serine metabolic process | The chemical reactions and pathways involving L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid. |
| maternal process involved in female pregnancy | A reproductive process occurring in the mother that allows an embryo or fetus to develop within it. |
| negative regulation of apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. |
| regulation of nitric oxide mediated signal transduction | Any process that modulates the rate, frequency or extent of nitric oxide mediated signal transduction. Nitric oxide mediated signal transduction is The series of molecular signals mediated by the detection of nitric oxide (NO). |
| response to folic acid | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a folic acid stimulus. |
| superoxide metabolic process | The chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species. |
| 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. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPSGTSQCED | GSAGGFQHLD | MHSEKRQLEK | GPSGDKDRVW | IRPDTPSRCT | WQLGRAMADS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PHYHTVLTKS | PKILPDILRK | IGNTPMVRIN | KISKNAGLKC | ELLAKCEFFN | AGGSVKDRIS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LRMIEDAERA | GNLKPGDTII | EPTSGNTGIG | LALAAAVKGY | RCIIVMPEKM | SMEKVDVLRA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LGAEIVRTPT | NARFDSPESH | VGVAWRLKNE | IPNSHILDQY | RNASNPLAHY | DDTAEEILQQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CDGKLDMLVA | SAGTGGTITG | IARKLKEKCP | GCKIIGVDPE | GSILAEPEEL | NQTEQTAYEV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EGIGYDFIPT | VLDRAVVDKW | FKSNDEDSFA | FARMLIAQEG | LLCGGSSGSA | MAVAVKAARE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LQEGQRCVVI | LPDSVRNYMS | KFLSDKWMLQ | KGFMKEELSV | KRPWWWRLRV | QELSLSAPLT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VLPTVTCEDT | IAILREKGFD | QAPVVNESGA | ILGMVTLGNM | LSSLLAGKVR | PSDEVCKVLY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KQFKPIHLTD | TLGTLSHILE | MDHFALVVHE | QIQSRDQAWS | GVVGGPTDCS | NGMSSKQQMV |
| 550 | 560 | ||||
| FGVVTAIDLL | NFVAAREQTQ | T |