S-adenosylhomocysteine hydrolase [Q4Q124] | |
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Systematic Name | LmjF.36.3910 [Leishmania major] |
Gene Name | LMJF_36_3910 |
Molecular Weight | 47829 Da |
Protein Sequence Size | 437 |
Function | |
Charge | -3.5 |
Isoelectric Point | 5.9796 pH |
Description | S-adenosylhomocysteine hydrolase (EC 1.16.1.8). |
Subcellular Location | N.A.[Predict] |
E. C. Number | 1.16.1.8; 3.3.1.1 |
Sequence | >tr|Q4Q124|Q4Q124_LEIMA S-adenosylhomocysteine hydrolase (EC 1.16.1.8) - Leishmania major ADYKVKDISLAEWGRKAIELAENEMPGLMELRREYGPSQPLKGAKIAGCLHMTVQTAVLI ETLKALGAELRWSSCNIFSTQDNAAAAIAKTGVPVFAWKGETDEEYEWCIAQTVKGFSGD GLPNMILDDGGDLTNLVIDRYPELVPKIFGISEETTTGVKNLYKRLSKGNLPISAINVND SVTKSKFDNLYGCRESLVDGIKRATDVMIAGKTCCVCGYGDVGKGCAAALRAFGARVVVT EVDPINALQASMEGYQVALVEDVMADAHIFVTTTGNDDIITSDHFPHMRDDAIVCNIGHF DTEIQVGWLEANAKEHVEIKPQVDRYTMENGRHIILLAKGRLVNLGCASGHPSFVMSNSF TNQVLAQIELWSNRDNGKYPRGDKAGVFFLPKALDEKVAALHLAHVGAKLTKLTPKQAEY INCPVNGPFKPDHYRY |
DNA Sequence | >LmjF36.3910 |||S-adenosylhomocysteine hydrolase|Leishmania major|chr 36|||Manual ATGGCGGACT ACAAGGTAAA AGACATCAGC CTCGCGGAGT GGGGCCGCAA GGCGATCGAGCTCGCGGAAA ACGAGATGCC CGGTCTGATG GAGCTGCGCC GCGAGTACGG ACCCTCCCAGCCGCTGAAGG GCGCCAAGAT TGCCGGCTGC CTGCACATGA CCGTACAGAC TGCCGTGCTGATCGAGACCC TCAAGGCCCT CGGTGCGGAG CTGCGCTGGT CGTCGTGCAA CATCTTTTCCACTCAGGATA ACGCCGCTGC GGCCATTGCC AAGACTGGCG TACCGGTGTT TGCGTGGAAGGGTGAGACAG ACGAGGAGTA TGAGTGGTGC ATCGCCCAGA CAGTGAAGGG CTTCAGCGGTGACGGTCTGC CGAACATGAT CCTCGACGAC GGTGGCGACC TCACGAATCT GGTGATCGACCGCTACCCCG AGCTCGTGCC CAAGATCTTC GGTATCTCCG AGGAGACCAC GACGGGTGTGAAGAACCTGT ACAAGCGCCT GAGCAAGGGC AACCTCCCCA TCTCCGCCAT CAACGTTAACGACAGCGTGA CGAAGAGCAA GTTCGACAAC CTTTACGGCT GCCGAGAGTC CTTGGTGGACGGCATCAAGC GCGCCACGGA TGTCATGATT GCCGGCAAGA CGTGCTGCGT GTGCGGATACGGTGATGTTG GTAAGGGCTG CGCCGCCGCC CTGCGCGCCT TCGGCGCTCG CGTTGTGGTAACGGAGGTGG ACCCTATCAA TGCCCTTCAG GCCTCCATGG AGGGCTACCA GGTCGCTCTGGTCGAAGACG TCATGGCCGA TGCGCACATC TTCGTGACGA CCACCGGCAA CGATGACATCATCACCTCTG ACCACTTCCC TCACATGCGC GACGACGCCA TTGTGTGCAA CATCGGCCACTTCGACACGG AGATCCAGGT GGGATGGCTT GAGGCAAACG CCAAAGAGCA CGTGGAAATCAAGCCTCAGG TGGACCGCTA TACCATGGAG AACGGCCGTC ACATCATCCT GCTGGCTAAGGGCCGCCTGG TCAACCTCGG CTGCGCCAGC GGTCACCCGT CCTTCGTGAT GTCCAACTCCTTCACGAACC AGGTGCTGGC TCAGATCGAG CTCTGGAGCA ACCGCGACAA CGGCAAGTACCCGCGCGGTG ACAAGGCCGG CGTGTTCTTC CTGCCCAAGG CGCTCGATGA GAAGGTCGCCGCCCTCCACC TCGCCCACGT CGGCGCCAAG CTGACAAAAC TGACCCCGAA GCAGGCCGAGTACATCAACT GCCCGGTCAA CGGCCCGTTC AAGCCGGACC ACTACCGCTA CTAA |
S-adenosylhomocysteine hydrolase Q4Q124] | |
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Metabolite Information | L-serine biosynthesis; one-carbon compound metabolism |
Molecular Function | |
Biochemical Pathway | |
Regulatory Pathway | |
KEGG Pathways | K01251 |
Orthologs | ||||
Homologs | GI | Percent Identity | Evalue | Score |
Homo sapiens | S-adenosylhomocysteine hydrolase [Homo sapiens] | 71 | 1e-179 | 626 |
DEG Information | ||||
DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
YER043c S-adenosyl-L-homocysteine hydrolase | Saccharomyces cerevisiae | 67% | 1e-171 | 593 |
Post Translational Modification | ||||
PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
PDOC00016 | Cell attachment sequence | 382-384 | PS00016 | |
PDOC00021 | EGF-like domain signatures and profile | 216-227; | PS00022 | |
PDOC00595 | Formate--tetrahydrofolate ligase signatures | 180-183; | PS00722 | |
PDOC00603 | S-adenosyl-L-homocysteine hydrolase signatures | 75-89; | PS00738 | |
PDOC00603 | S-adenosyl-L-homocysteine hydrolase signatures | 212-229; | PS00739 | |
Acylation | N-myristoylation site | 44-49; 131-136; 193-198; 201-206; 226-231; 347-352; 408-413; | PS00008 | |
Amidation | Amidation site | 14-17; | PS00009 | |
Glycosylation | N-glycosylation site | 180-183; | PS00001 | |
Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 165-168; 203-206; | PS00004 | |
Phosphorylation | Casein kinase II phosphorylation site | 10-13; 80-83; 103-106; 186-189; 197-200; 241-244; 275-278; 373-376; | PS00006 | |
Phosphorylation | Protein kinase C phosphorylation site | 63-65; 114-116; 373-375; 415-417; | PS00005 | |
Phosphorylation | Tyrosine kinase phosphorylation site | 100-107; 185-192; | PS00007 |
S-adenosylhomocysteine hydrolase [Q4Q124] | ||
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Model Information | ||
Template PDB ID | 2h5lH | |
Percent Identity | 71% | |
Target Region | 1-437 | |
Template Region | 2-430 |
Domain Information | ||
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Domains | Start | End |
Active Site Information | ||
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Residue | Active Site Number | Functional Part |
HIS | 52 | Sidechain |
ASP | 130 | Sidechain |
LYS | 185 | Sidechain |
ASP | 189 | Sidechain |
ASN | 190 | Sidechain |
CYS | 194 | Sidechain |
HIS | 300 | Sidechain |
Co-Factor | |
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Metal | Description |
NAD | Binds 1 NAD per subunit |
Ligands | |||||
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CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
2R,3R)-4-(4-AMINO-1H-IMIDAZO[4,5-C]PYRIDIN- 1-YL)-2,3-DIHYDROXYBUTANOIC ACID | 252.227 | C10 H12 N4 O4 | O=C(O)C(O)C(O)Cn1c2ccnc(c2nc1)N | 2h5l | |
NICOTINAMIDE-ADENINE-DINUCLEOTIDE | 663.425 | C21 H27 N7 O14 P2 | c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N | 2h5l |
Mutational Information | ||
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Residue | Feature | Description |
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Modeled Protein | Template Structure |
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+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/805014/Q4Q124.pdb 2.0 437 = residues | | = | +| Ramachandran plot: 95.3% core 4.5% allow 0.3% gener 0.0% = disall | | = | +| All Ramachandrans: 3 labelled residues (out of 435) = | +| Chi1-chi2 plots: 1 labelled residues (out of 252) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 3.1 Bad contacts: = 9 | *| Bond len/angle: 8.2 Morris et al class: 1 = 1 2 | | = | | G-factors Dihedrals: 0.09 Covalent: -0.10 Overall: = 0.02 | | = | | M/c bond lengths: 99.3% within limits 0.7% highlighted = | *| M/c bond angles: 94.3% within limits 5.7% highlighted 1 off = graph | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |