P-POD: Princeton Protein Orthology Database: GO3/Jaccard288

This family has 64 members: 12 Arabidopsis thaliana, 13 Caenorhabditis elegans, 2 Danio rerio, 5 Dictyostelium discoideum, 2 Drosophila melanogaster, 4 Escherichia coli, 5 Gallus gallus, 4 Homo sapiens, 4 Mus musculus, 4 Rattus norvegicus, 5 Saccharomyces cerevisiae, 4 Schizosaccharomyces pombe.

• Protein Family
• Functional Conservation (6)
• Download Files (5)
• Disease References (7)

Interactive Java Applets: Notung Tree Analysis · Jalview Alignment

64 members.

Organism	Protein (Synonyms)	Description	AmiGO
A. thaliana	NCBI:NP_188885.2 · TAIR:locus:2077041 (F16J14.18 · AT3G22460 · OASA2)	O-ACETYLSERINE (THIOL) LYASE (OAS-TL) ISOFORM A1
A. thaliana	NCBI:NP_851022.1 · TAIR:locus:2080417 (ATCS-C · OASC · F24G16.30 · AT3G59760)	CSase C · ARABIDOPSIS THALIANA CYSTEINSYNTHASE-C · O-ACETYLSERINE (THIOL) LYASE ISOFORM C
A. thaliana	NCBI:NP_191703.1 · TAIR:locus:2082837 (ARATH;BSAS3;1 · AT3G61440 · ATCYSC1 · F2A19.40)	beta-substituted Ala synthase 3;1 · CYSTEINE SYNTHASE
A. thaliana	NCBI:NP_193224.1 · TAIR:locus:2130419 (ATCYS-3A · CYTACS1 · OASA1 · DL3480C · FCAALL.34 · AT4G14880)	O-acethylserine sulfhydrylase · O-ACETYLSERINE (THIOL)LYASE · O-ACETYLSERINE (THIOL) LYASE (OAS-TL) ISOFORM A1
A. thaliana	NCBI:NP_181903.1 · TAIR:locus:2043964 (CPACS1 · OASB · ATCS-B · F18O19.14 · AT2G43750 · ACS1)	CSASE B · ARABIDOPSIS THALIANA CYSTEIN SYNTHASE-B · ARABIDOPSIS CYSTEINE SYNTHASE 1 · CHLOROPLAST O-ACETYLSERINE SULFHYDRYLASE 1 · O-ACETYLSERINE (THIOL) LYASE B · CYSTEINE SYNTHASE
A. thaliana	NCBI:NP_974843.1 · TAIR:locus:2143754 (F15F15_100 · F15F15.100 · AT5G28030)
A. thaliana	NCBI:NP_566243.1 · TAIR:locus:2114804 (T9J14_11 · AT3G04940 · T9J14.11 · ATCYSD1)	CYSTEINE SYNTHASE
A. thaliana	NCBI:NP_175984.1 · TAIR:locus:2012110 (F14J16.13 · F14J16_13 · AT1G55880)
A. thaliana	NCBI:NP_851087.1 · TAIR:locus:2143814 (F15F15_90 · AT5G28020 · F15F15.90 · ATCYSD2)	CYSTEINE SYNTHASE
A. thaliana	NCBI:NP_192901.2 · TAIR:locus:2139767 (T5C23_70 · ATSR · AT4G11640 · T5C23.70)	ARABIDOPSIS THALIANA SERINE RACEMASE
A. thaliana	NCBI:NP_187616.1 · TAIR:locus:2100078 (T22K18.12 · OMR1 · AT3G10050)	THREONINE DEHYDRATASE/DEAMINASE · L-O-METHYLTHREONINE RESISTANT 1
A. thaliana	NCBI:NP_187013.1 · TAIR:locus:2096454 (CS26 · AT3G03630 · T12J13.9 · T12J13_9)	O-ACETYLSERINE (THIOL) LYASE
C. elegans	WB:WBGene00008732 (F13B12.4) · UniProtKB:Q19374
C. elegans	WB:WBGene00019962 (R08E5.2) · UniProtKB:O01592
C. elegans	WB:WBGene00008490 · UniProtKB:O01982
C. elegans	WB:WBGene00019094 · UniProtKB:O16282
C. elegans	WB:WBGene00019096 (F59A7.9) · UniProtKB:O16284
C. elegans	WB:WBGene00010759 (K10H10.2) · UniProtKB:O45679 (K10H10.2)	Protein K10H10.2, confirmed by transcript evidence
C. elegans	WB:WBGene00010456 (K01C8.1) · UniProtKB:Q21080
C. elegans	WB:WBGene00013866 (ZC373.1) · UniProtKB:Q23264
C. elegans	WB:WBGene00007653 (C17G1.7) · UniProtKB:Q93244
C. elegans	WB:WBGene00011353 (T01H8.2) · UniProtKB:Q93968
C. elegans	WB:WBGene00021787 (Y51H7C.9) · UniProtKB:Q95XY8
C. elegans	WB:WBGene00020797 · UniProtKB:Q965I8
C. elegans	WB:WBGene00018783 (F54A3.4) · UniProtKB:Q9N4K2
D. rerio	UniProtKB:Q5EI65 · ZFIN:ZDB-GENE-021030-3 (cbsb)	cystathionine-beta-synthase b
D. rerio	UniProtKB:A9JT04 · ZFIN:ZDB-GENE-050417-367 (cbsa)	cystathionine-beta-synthase a
D. discoideum	UniProtKB:P46794 · dictyBase:DDB_G0267386 (cysB)	cystathionine beta-synthase
D. discoideum	UniProtKB:Q54CN7 · dictyBase:DDB_G0292840 (cysK)	cysteine synthase
D. discoideum	UniProtKB:Q86B06 · dictyBase:DDB_G0272787 (sds)	L-serine ammonia-lyase, L-serine dehydratase, serine deaminase
D. discoideum	UniProtKB:Q54HH2 · dictyBase:DDB_G0289463 (DDB_G0289463)	threonine ammonia-lyase, serine/threonine dehydratase, threonine deaminase
D. discoideum	UniProtKB:Q86AP7 · dictyBase:DDB_G0277245 (DDB_G0277245)	threonine ammonia-lyase, serine/threonine dehydratase, threonine deaminase
D. melanogaster	FB:FBgn0037684 (CT24308 · CG8129) · UniProtKB:Q9VHF0
D. melanogaster	FB:FBgn0031148 (CG1753) · UniProtKB:Q9VRD9
E. coli	UniProtKB:P0ABK5 · ECOLI:ACSERLYA-MONOMER (ssi5 · cysZ · b2414 · cysK · CysK · ECK2409)
E. coli	UniProtKB:P16703 · ECOLI:ACSERLYB-MONOMER (b2421 · CysM · ECK2416 · cysM)
E. coli	UniProtKB:P04968 · ECOLI:THREDEHYDSYN-MONOMER (b3772 · ECK3764 · ile · ilvA · IlvA)
E. coli	UniProtKB:P0AGF6 · ECOLI:THREDEHYDCAT-MONOMER (Tdc · ECK3106 · tdcB · tdc · b3117 · TdcB)
G. gallus	NCBI:XP_416751 · ENTREZ:418544
G. gallus	NCBI:XP_416752 · ENTREZ:418545
G. gallus	NCBI:XP_415319 · ENTREZ:417030
G. gallus	NCBI:XP_001234891 · ENTREZ:771635
G. gallus	ENTREZ:423635 · NCBI:XP_421519
H. sapiens	ENSEMBL:ENSG00000160200 · UniProtKB:P35520 (P35520 · IPI00219352 · CBS · CBS_HUMAN · IPI00219649)	Cystathionine beta-synthase
H. sapiens	ENSEMBL:ENSG00000135094 · UniProtKB:P20132 (SDHL_HUMAN · P20132 · SDS · SDH · IPI00022201)	L-serine dehydratase
H. sapiens	ENSEMBL:ENSG00000139410 · UniProtKB:Q96GA7 (SDSL · IPI00062419 · SDSL_HUMAN · Q96GA7)	Serine dehydratase-like
H. sapiens	ENSEMBL:ENSG00000167720 · UniProtKB:Q9GZT4 (SRR_HUMAN · IPI00030328 · SRR · Q9GZT4)	Serine racemase
M. musculus	UniProtKB:Q91WT9 · MGI:MGI:88285 (Cbs · HIP4)	cystathionine beta-synthase
M. musculus	UniProtKB:Q8VBT2 · MGI:MGI:98270 (Sds · SDH)	serine dehydratase
M. musculus	UniProtKB:Q8R238 · MGI:MGI:2182607 (SDS-RS1 · SDH1 · Sdsl)	serine dehydratase-like
M. musculus	UniProtKB:Q9QZX7 · MGI:MGI:1351636 (Srr)	serine racemase
R. norvegicus	NCBI:XP_001079897 · RGD:1309192
R. norvegicus	RGD:2287 (Cbs) · UniProtKB:P32232 (IPI00231549 · IPI00231548 · P32232 · Cbs · IPI00214299 · CBS_RAT)	cystathionine beta synthase · Cystathionine beta-synthase
R. norvegicus	RGD:67376 (Sds) · UniProtKB:P09367 (IPI00231470 · Sds · P09367 · SDHL_RAT · IPI00193769)	serine dehydratase · L-serine dehydratase/L-threonine deaminase
R. norvegicus	UniProtKB:Q76EQ0 · RGD:735094 (Srr)	serine racemase
S. cerevisiae	UniProtKB:P32582 · SGD:S000003387 (CYS4 · VMA41 · NHS5 · YGR155W · STR4)	Cystathionine beta-synthase, catalyzes the synthesis of cystathionine from serine and homocysteine, the first committed step in cysteine biosynthesis
S. cerevisiae	UniProtKB:P53206 · SGD:S000003244 (YGR012W)	Putative cysteine synthase, localized to the mitochondrial outer membrane
S. cerevisiae	UniProtKB:P36007 · SGD:S000001701 (SRY1 · YKL218C)	3-hydroxyaspartate dehydratase, deaminates L-threo-3-hydroxyaspartate to form oxaloacetate and ammonia
S. cerevisiae	UniProtKB:P25379 · SGD:S000000569 (YCL064C · CHA1)	Catabolic L-serine (L-threonine) deaminase, catalyzes the degradation of both L-serine and L-threonine
S. cerevisiae	UniProtKB:P00927 · SGD:S000000888 (YER086W · ILV1 · ISO1)	Threonine deaminase, catalyzes the first step in isoleucine biosynthesis
S. pombe	UniProtKB:O59701 · GeneDB_Spombe:SPBC36.04 (cys11 · SPBC36.04 · cys1a)	cysteine synthase
S. pombe	UniProtKB:P87131 · GeneDB_Spombe:SPAC3A12.17c (cys1b · SPAC3A12.17c · cys12)	cysteine synthase Cys12
S. pombe	UniProtKB:O94634 · GeneDB_Spombe:SPBC1677.03c (SPBC1677.03c)	threonine ammonia-lyase
S. pombe	UniProtKB:O59791 · GeneDB_Spombe:SPCC320.14 (SPCC320.14 · SPCC330.15c)	threo-3-hydroxyaspartate ammonia-lyase · threo-3-hydroxyaspartate ammonia-lyase (predicted)

Protein	Publication	Curator Notes
UniProtKB:P32582 · SGD:S000003387	8528202 Kruger WD, et al. A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61.	The H. sapiens protein P35520 complements a homologous mutation in S. cerevisiae.
UniProtKB:P32582 · SGD:S000003387	8022826 Kruger WD, et al. A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6614-8.	The H. sapiens protein P35520 complements a homologous mutation in S. cerevisiae.
UniProtKB:P32582 · SGD:S000003387	8022826 Kruger WD, et al. A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6614-8.	The H. sapiens protein CBS complements a homologous mutation in S. cerevisiae.
UniProtKB:P32582 · SGD:S000003387	8528202 Kruger WD, et al. A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61.	The H. sapiens protein CBS complements a homologous mutation in S. cerevisiae.
UniProtKB:P32582 · SGD:S000003387	8528202 Kruger WD, et al. A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61.	The H. sapiens protein CBS complements a homologous mutation in S. cerevisiae.
UniProtKB:P32582 · SGD:S000003387	22267502 Mayfield JA, et al. Surrogate genetics and metabolic profiling for characterization of human disease alleles. Genetics. 2012 Apr;190(4):1309-23.	The H. sapiens protein CBS complements a homologous mutation in S. cerevisiae.

Description	Suffix
Sequences in this family	.fasta
mafft aligned Fasta file	.afasta
phyml newick file	.newick
Notung rooted & rearranged newick file	.newick.rooting.0.rearrange.0
Notung Homolog Table	.newick.rooting.0.rearrange.0.homologs.csv

OMIM (2)
ENSEMBL:ENSG00000160200 · UniProtKB:P35520	+236200 HOMOCYSTINURIA;;CYSTATHIONINE BETA-SYNTHASE DEFICIENCY;;CBS DEFICIENCYCYSTATHIONINE BETA-SYNTHASE, INCLUDED; CBS, INCLUDED;;HOMOCYSTINURIA, PYRIDOXINE-RESPONSIVE, INCLUDED
UniProtKB:P32582 · SGD:S000003387	#603174 HOMOCYSTEINEMIA
SGD Disease Papers (5)
UniProtKB:P32582 · SGD:S000003387	9590298 Shan X and Kruger WD (1998) Correction of disease-causing CBS mutations in yeast. Nat Genet 19(1):91-3
	9300813 Foury F (1997) Human genetic diseases: a cross-talk between man and yeast. Gene 195(1):1-10
	8022826 Kruger WD and Cox DR (1994) A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A 91(14):6614-8
	12455965 Lo SC, et al. (2002) Molecular characterization of a cystathionine beta-synthase gene, CBS1, in Magnaporthe grisea. Eukaryot Cell 1(2):311-4
	10956046 Jhee KH, et al. (2000) Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation. Biochemistry 39(34):10548-56