Summary: SOR/SNZ family
SOR/SNZ family Provide feedback
Members of this family are enzymes involved in a new pathway of pyridoxine/pyridoxal 5-phosphate biosynthesis . This family was formerly known as UPF0019.
Braun EL, Fuge EK, Padilla PA, Werner-Washburne M; , J Bacteriol 1996;178:6865-6872.: A stationary-phase gene in Saccharomyces cerevisiae is a member of a novel, highly conserved gene family. PUBMED:8955308 EPMC:8955308
Ehrenshaft M, Bilski P, Li MY, Chignell CF, Daub ME; , Proc Natl Acad Sci U S A 1999;96:9374-9378.: A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis. PUBMED:10430950 EPMC:10430950
Osmani AH, May GS, Osmani SA; , J Biol Chem 1999;274:23565-23569.: The extremely conserved pyroA gene of Aspergillus nidulans is required for pyridoxine synthesis and is required indirectly for resistance to photosensitizers. PUBMED:10438537 EPMC:10438537
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001852
Snz1p is a highly conserved protein involved in growth arrest in Saccharomyces cerevisiae (Baker's yeast) [PUBMED:8955308]. Sor1 (singlet oxygen resistance) is essential in pyridoxine (vitamin B6) synthesis in Cercospora nicotianae and Aspergillus flavus. Pyridoxine quenches singlet oxygen at a rate comparable to that of vitamins C and E, two of the most highly efficient biological antioxidants, suggesting a previously unknown role for pyridoxine in active oxygen resistance [PUBMED:10430950].
|Biological process||pyridoxal phosphate biosynthetic process (GO:0042823)|
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a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This large superfamily of TIM barrel enzymes all contain a common phosphate binding site. The phosphate is found in a variety of cofactors and ligands such as FMN [1,2].
The clan contains the following 57 members:Ala_racemase_N ALAD Aldolase AP_endonuc_2 BtpA CdhD CutC DAHP_synth_1 DAHP_synth_2 DeoC DHDPS DHO_dh DHquinase_I DUF1341 DUF2090 DUF556 DUF561 DUF692 DUF993 Dus F_bP_aldolase FMN_dh G3P_antiterm Glu_syn_central Glu_synthase His_biosynth HMGL-like IGPS IMPDH Lys-AminoMut_A MtrH NanE NAPRTase NeuB NMO OAM_alpha OMPdecase Orn_Arg_deC_N Oxidored_FMN PcrB PdxJ PRAI Pterin_bind QRPTase_C Radical_SAM RhaA Ribul_P_3_epim SOR_SNZ Tagatose_6_P_K ThiC_Rad_SAM ThiG TIM TMP-TENI Transaldolase Trp_syntA UvdE UxuA
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Pfam-B_2034 (release 4.1)|
|Author:||Belitsky B, Bateman A|
|Number in seed:||136|
|Number in full:||9149|
|Average length of the domain:||204.50 aa|
|Average identity of full alignment:||75 %|
|Average coverage of the sequence by the domain:||69.59 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There are 4 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the SOR_SNZ domain has been found. There are 74 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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