DCAMP_TRYBB
ID DCAMP_TRYBB Reviewed; 325 AA.
AC A5HNV6;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Inactive S-adenosylmethionine decarboxylase prozyme {ECO:0000303|PubMed:17485680};
DE Short=AdoMetDC prozyme {ECO:0000305|PubMed:17485680};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702 {ECO:0000305};
RN [1] {ECO:0000312|EMBL:ABQ23689.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, INTERACTION WITH ADOMETDC,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=427 {ECO:0000312|EMBL:ABQ23689.1};
RX PubMed=17485680; DOI=10.1073/pnas.0701111104;
RA Willert E.K., Fitzpatrick R., Phillips M.A.;
RT "Allosteric regulation of an essential trypanosome polyamine biosynthetic
RT enzyme by a catalytically dead homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8275-8280(2007).
RN [2] {ECO:0000305}
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=18949025; DOI=10.1371/journal.ppat.1000183;
RA Willert E.K., Phillips M.A.;
RT "Regulated expression of an essential allosteric activator of polyamine
RT biosynthesis in African trypanosomes.";
RL PLoS Pathog. 4:E1000183-E1000183(2008).
CC -!- FUNCTION: Probably has no catalytic activity due to the loss of several
CC residues required for processing and catalysis (PubMed:17485680). Forms
CC a complex with S-adenosylmethionine decarboxylase AdoMetDC which is
CC essential to activate AdoMetDC (PubMed:17485680, PubMed:18949025).
CC Required for the biosynthesis of the polyamine spermidine
CC (PubMed:18949025). Required for growth and survival during the
CC bloodstream life cycle stage (PubMed:18949025).
CC {ECO:0000269|PubMed:17485680, ECO:0000269|PubMed:18949025}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1. {ECO:0000269|PubMed:17485680, ECO:0000269|PubMed:18949025}.
CC -!- SUBUNIT: Forms a heterodimer with S-adenosylmethionine decarboxylase
CC AdoMetDC; heterodimerization is required to activate AdoMetDC.
CC {ECO:0000269|PubMed:17485680}.
CC -!- DEVELOPMENTAL STAGE: Expressed during both bloodstream (BF) and
CC procyclic insect (PF) life cycle stages. {ECO:0000269|PubMed:17485680}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the bloodstream life
CC cycle stage causes cell growth arrest followed by death. Putrescine
CC levels are increased and the production of spermidine, glutathione,
CC glutathionyl-spermidine and trypanothione is severely reduced. In
CC addition, protein expression levels of ornithine carboxylase (ODC) are
CC increased. {ECO:0000269|PubMed:18949025}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; EF545594; ABQ23689.1; -; mRNA.
DR PDB; 6BM7; X-ray; 2.98 A; E/F=1-325.
DR PDBsum; 6BM7; -.
DR AlphaFoldDB; A5HNV6; -.
DR SMR; A5HNV6; -.
DR EnsemblProtists; AAZ12005; AAZ12005; Tb927.6.4470.
DR HOGENOM; CLU_856601_0_0_1; -.
DR OMA; AFHQLLF; -.
DR UniPathway; UPA00331; UER00451.
DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:1901307; P:positive regulation of spermidine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:UniProtKB.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
DR GO; GO:0019342; P:trypanothione biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR001985; S-AdoMet_decarboxylase.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR PANTHER; PTHR11570; PTHR11570; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Polyamine biosynthesis; Spermidine biosynthesis.
FT CHAIN 1..325
FT /note="Inactive S-adenosylmethionine decarboxylase prozyme"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438856"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:6BM7"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 36..47
FT /evidence="ECO:0007829|PDB:6BM7"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6BM7"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:6BM7"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 79..91
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6BM7"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:6BM7"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:6BM7"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:6BM7"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 300..310
FT /evidence="ECO:0007829|PDB:6BM7"
FT STRAND 315..323
FT /evidence="ECO:0007829|PDB:6BM7"
SQ SEQUENCE 325 AA; 36303 MW; 89FB77915E12F2E4 CRC64;
MSVTRINQQT ECPSSVHDLV SCWGGCTQSK TSTDSGLEKR FELNFAQPVD IGTVTVKQLA
SVMERAGESL RQNSAELGIH TLKFDRSLLV FTAKQIVVRS SVSVMLHEAV HPMLELMRSH
NIIVDWASFM RVNYGSPWDM TSETSDIMAH EYAELKSAFP TGHPYLAGPV DRDHCFYFVY
DGIDRDPSSC RRENDVQINV YMYNVQADDE YDLDGNTKEQ QLLVSHCAGE YETLRVSTYG
STHPFASFET NAVSAASDIT KIVNGLLKKF YPERVLLVLL QDRDAQGTTA CGVMDRLEGF
TVVHRGANHF GGGYVFHQAT YARSA
