C5DYG3 (C5DYG3_ZYGRC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
S-adenosylmethionine decarboxylase proenzyme PIRNR PIRNR001355
EC=4.1.1.50 PIRNR PIRNR001355

Gene names

Ordered Locus Names:

ZYRO0F12804g

Organism

Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229) (Candida mogii) [Complete proteome]

Taxonomic identifier

559307 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Zygosaccharomyces › Zygosaccharomyces rouxii

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. PIRNR PIRNR001355
Cofactor	Pyruvoyl group By similarity. PIRNR PIRNR001355
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. PIRNR PIRNR001355
Sequence similarities	Belongs to the eukaryotic AdoMetDC family. PIRNR PIRNR001355

Ontologies

Keywords
Biological process	Polyamine biosynthesis PIRNR PIRNR001355 Spermidine biosynthesis PIRNR PIRNR001355
Ligand	Pyruvate PIRNR PIRNR001355 S-adenosyl-L-methionine PIRNR PIRNR001355 Schiff base PIRNR PIRNR001355
Molecular function	Decarboxylase PIRNR PIRNR001355 Lyase
PTM	Zymogen PIRNR PIRNR001355
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	S-adenosylmethioninamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW spermine biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	adenosylmethionine decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	94	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity PIRSR PIRSR001355-1
	Active site	108	1	Proton donor; for catalytic activity By similarity PIRSR PIRSR001355-1
	Active site	286	1	Proton acceptor; for processing activity By similarity PIRSR PIRSR001355-1
	Active site	300	1	Proton acceptor; for processing activity By similarity PIRSR PIRSR001355-1
Amino acid modifications
	Modified residue	94	1	Pyruvic acid (Ser); by autocatalysis By similarity PIRSR PIRSR001355-3

Sequences

	Sequence		Length	Mass (Da)
	C5DYG3 [UniParc]. Last modified July 28, 2009. Version 1. Checksum: 4A0B0FAB3D5DD777	FASTA	399	45,972
	10 20 30 40 50 60 MTVTINELTN HTYIDKELSA ALDSTEAFEG PEKLLEIWFY AHSDDIPDTN VSANKRTLRD 70 80 90 100 110 120 IPLDQWVEIL KLVKCEVLSI KSTKQMHAFL LSESSLFIYD HRLTLKTCGT TTTLLCLERL 130 140 150 160 170 180 LDVVQEQLGW KMKTSNSDGK YSPFKVFYSR RCFMFPLKQR SIHKSWSSEV DYLNQFFSNG 190 200 210 220 230 240 RSYLVGRNDQ SNHWNLYVTE SQPTTTASNH PQNDETLEVL MTGLDPFRAK QFVSNRNIDP 250 260 270 280 290 300 TSSSGDEGHL LGYNITKSTG LDKIYDNRTQ VNFTHDAFAF TPCGYSSNMV LDEQFYYTLH 310 320 330 340 350 360 VTPEKGWSYA SFESNVPVRQ VSNNEQNNCQ VLANVLAVFQ PMEFCLTFFA KDCNAVSQLT 370 380 390 QLIQSMKNYS KRDKIIYDLD DYQLLYMRFE KNESTTTVG

References

[1]

"Comparative genomics of protoploid Saccharomycetaceae." The Genolevures Consortium Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V., Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V., Vacherie B., Val M.-E. , Fulton R.S., Minx P., Wilson R., Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E. Genome Res. 19:1696-1709(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928178 Genomic DNA. Translation: CAR28824.1.
RefSeq	XP_002497757.1. XM_002497712.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	559307.ZYRO0F12804g.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8205524.
KEGG	zro:ZYRO0F12804g.
Phylogenomic databases
eggNOG	NOG77566.
HOGENOM	HOG000159915.
KO	K01611.
OrthoDB	EOG4Q8867.
Enzyme and pathway databases
UniPathway	UPA00331; UER00451.
Family and domain databases
Gene3D	3.60.90.10. 1 hit.
InterPro	IPR001985. S-AdoMet_decarboxylase. IPR018167. S-AdoMet_decarboxylase_subgr. IPR016067. S-AdoMet_deCO2ase_core. IPR018166. S-AdoMet_deCO2ase_CS. [Graphical view]
PANTHER	PTHR11570. PTHR11570. 1 hit.
Pfam	PF01536. SAM_decarbox. 1 hit. [Graphical view]
PIRSF	PIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAM	SSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMs	TIGR00535. SAM_DCase. 1 hit.
PROSITE	PS01336. ADOMETDC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C5DYG3_ZYGRC

Accession

Primary (citable) accession number: C5DYG3

Entry history

Integrated into UniProtKB/TrEMBL:	July 28, 2009
Last sequence update:	July 28, 2009
Last modified:	May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)