ID A0A024VK72_PLAFA Unreviewed; 1564 AA.
AC A0A024VK72;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Adenosylmethionine decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFFCH_03822 {ECO:0000313|EMBL:ETW28693.1};
OS Plasmodium falciparum FCH/4.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036724 {ECO:0000313|EMBL:ETW28693.1, ECO:0000313|Proteomes:UP000030656};
RN [1] {ECO:0000313|EMBL:ETW28693.1, ECO:0000313|Proteomes:UP000030656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW28693.1,
RC ECO:0000313|Proteomes:UP000030656};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum FCH/4.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW28693.1, ECO:0000313|Proteomes:UP000030656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW28693.1,
RC ECO:0000313|Proteomes:UP000030656};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum FCH/4.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50};
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1. {ECO:0000256|ARBA:ARBA00004911}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|ARBA:ARBA00008872, ECO:0000256|RuleBase:RU003737}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family.
CC {ECO:0000256|ARBA:ARBA00008466}.
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DR EMBL; KI928022; ETW28693.1; -; Genomic_DNA.
DR EnsemblProtists; ETW28693; ETW28693; PFFCH_03822.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000030656; Unassembled WGS sequence.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:InterPro.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.10; Alanine racemase; 2.
DR Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 2.
DR InterPro; IPR048283; AdoMetDC-like.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR002433; Orn_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR PANTHER; PTHR11482; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR PANTHER; PTHR11482:SF6; ORNITHINE DECARBOXYLASE 1-RELATED; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR Pfam; PF01536; SAM_decarbox; 2.
DR PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000030656}.
FT DOMAIN 847..1123
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 1290..1381
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT REGION 351..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1354
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 870
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 1564 AA; 183410 MW; A17C3C63F79B75B0 CRC64;
MNGIFEGIEK RVVIKLKESF FKGNRNVNSF LDIPKELWEE KLKYIGCSIV SEISEDKNER
RGERCRVYLL SESSLYIFDD SLFIKTCGKT RVLFFIPFVV DLLIYHMDNV GIIEKNCVYD
ETFIENEKFH NIAEFIKEHF LYCFFTHMNY RNKTKDGYFE QEYPHKSLED EKKFFEFFFK
NVQMYNTHLP MEKMHYIFFY SSDDVHMTDI ASTFKFCSEI HLFGINKYNE KNQFHDAYLN
NKSLNLFARV HEDNLKLYDS SDADKEVTTH IYSTRGTYED TGMVNCVDVI YKNESTLLNR
NNIENIPSIE NKESNNNSRC CHNNNYSGSC HNIVSVVPSE RNNDHVHHRH YEDTLNRSNI
SAEDNNRNAQ PEKEKDEDVR RDDEENKVLI KMIDTNLYEC INYNKESFLY NEFYFTPCGY
SCNVSEKNNY FCVHYSPEDS VSYVSVEVSS NLSCDRFLDF MHKQLNFYNG KYMFMINYVF
CEESNNMSKM VPDDDNNNYS SGKSCVYYQD LNKKEKEEYY RLNKKLRNDL FINSKQFYEL
HTFTERTVGF MRVQYFVYKL RDVVKCVEKE TLLARSSSCL FMFNNIKRND VHDDYVTKSS
NGGVIKQLTE RDVDDMYEYA LNFCKQNKIV VVDTNTFFFD ASKRKENLIK LEKIQTNEKD
EYEEKDEVYR MGNNELSSLD HLDSKNNLIH MYYEKNKCDI INKDDENSTI ATNNNDNNND
SSSYDKSITI SRSSSCNNSH LSYSSFDNNH GNEKMKDYIS VDENNNNNNN NNNKNNNVLL
TLQRNSDDEN GKDKDNEKND VSLENNMEKN YKEEIWNYYT KNKVEVKTLE KVLNENIDTS
VVCINLQKIL AQYVRFKKNL PHVTPFYSVK SNNDEVVIKF LYGLNCNFDC ASIGEISKVI
KLLPNLSRDR IIFANTIKSI NSLIYARKEN INLCTFDNLD ELKKIYKYHP KCSLILRINV
DFKNYKSYMS SKYGANEYEW EEMLLYAKKH NLNIVGVSFH VGSNTKNLFD FCLAIKLCRD
VFDMSSNMGF NFYIINLGGG YPEELEYDNA KKHDKIHYCT LSLQEIKKDI QKFLNEETFL
KTKYGYYSFE KISLAINMSI DHYFSHMKDN LRVICEPGRY MVAASSTLAV KIIGKRRPTF
QGIMLKDLKD HYDPLNFAQQ ENKKQDETKI NHNNDNNDNN SNDNNNNNNN QKGGQGNIMN
DLIITSTNDS TNKKNDHSSS QVIQNVSCTI RDKEGDNIKI NTHTINNPNI NGKENTVDGD
NINIAHKNIG NNFSSSNSKL GNITNIKKKV VNINDNRYNY FSYYVSDSIY GCFSGIIFDE
YNRCPIYVIK NKNNPNQNFM NFNLYLANVF GQSCDGLDMI NSITYLPECY INDWLLYEYA
GAYTFVSSSN FNGFKKCKKV YIFPESKPSL KGQPNKHCNN IQEQENKDEL INKDIPSNNK
TDNKENNHIP KNNPLNCNDN NQKNLQNIGN NKNKIRDEVL IIDEESVNLA IKEYVLKTIY
RKKNVDFLYE KLEFQQKDNL MVNRNIKYPS GLPPYLPDDC SVNTILPSWD IKYNFNSSKR
KIKK
//
