(data stored in ACNUC7421 zone)

HOGENOM: VULDI_1_PE1005

ID   VULDI_1_PE1005                       STANDARD;      PRT;   148 AA.
AC   VULDI_1_PE1005; E1QQ48;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE   Short=AdoMetDC; Short=SAMDC; EC=4.1.1 50; (VULDI_1.PE1005).
GN   Name=speH; OrderedLocusNames=Vdis_1031;
OS   VULCANISAETA DISTRIBUTA DSM 14429.
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Vulcanisaeta.
OX   NCBI_TaxID=572478;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS VULDI_1.PE1005.
CC       Vulcanisaeta distributa DSM 14429 chromosome, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:E1QQ48_VULDI
CC   -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to
CC       S-adenosylmethioninamine (dcAdoMet), the propylamine donor
CC       required for the synthesis of the polyamines spermine and
CC       spermidine from the diamine putrescine (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = (5-deoxy-5-
CC       adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).
CC   -!- COFACTOR: Pyruvoyl group (By similarity).
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-
CC       adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
CC       S-adenosyl-L-methionine: step 1/1.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged
CC       as a dimer of alpha/beta heterodimers (By similarity).
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation
CC       of the active enzyme involves a self-maturation process in which
CC       the active site pyruvoyl group is generated from an internal
CC       serine residue via an autocatalytic post-translational
CC       modification. Two non-identical subunits are generated from the
CC       proenzyme in this reaction, and the pyruvate is formed at the N-
CC       terminus of the alpha chain, which is derived from the carboxyl
CC       end of the proenzyme. The post-translation cleavage follows an
CC       unusual pathway, termed non-hydrolytic serinolysis, in which the
CC       side chain hydroxyl group of the serine supplies its oxygen atom
CC       to form the C-terminus of the beta chain, while the remainder of
CC       the serine residue undergoes an oxidative deamination to produce
CC       ammonia and the pyruvoyl group blocking the N-terminus of the
CC       alpha chain (By similarity).
CC   -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000216579 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E1QQ48; -.
DR   EMBL; CP002100; ADN50420.1; -; Genomic_DNA.
DR   RefSeq; YP_003901471.1; NC_014537.1.
DR   GeneID; 9751961; -.
DR   GenomeReviews; CP002100_GR; Vdis_1031.
DR   KEGG; vdi:Vdis_1031; -.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:HAMAP.
DR   GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00464; AdoMetDC_1; 1; -.
DR   InterPro; IPR003826; S-AdoMet_decarboxylase-bac/arc.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
DR   Gene3D; G3DSA:3.60.90.10; SAM_decarbox; 1.
DR   Pfam; PF02675; AdoMet_dc; 1.
DR   SUPFAM; SSF56276; S-AdenosylMet_decarbase_core; 1.
DR   TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
DR   HOGENOMDNA; VULDI_1.PE1005; -.
KW   S-adenosylmethionine decarboxylase proenzyme;
KW   Autocatalytic cleavage; Complete proteome; Decarboxylase; Lyase;
KW   Polyamine biosynthesis; Pyruvate; S-adenosyl-L-methionine;
KW   Schiff base; Spermidine biosynthesis; Zymogen.
SQ   SEQUENCE   148 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTTQTLIELG GRERNALVYG VHVYGNLYGC NRELLKDEVY LLKTVKEAAD IAGALVVSTF
     YYKFGVNGGI SVVAIVAESH ISIHTWPEHG YATVDVYTCG SHTNPMAAFE YIAKSLNAKK
     VEVFVSDRSY YADNNVNNNN ENSGENVS
//

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