ID A0A1F5DES4_9ARCH Unreviewed; 486 AA.
AC A0A1F5DES4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Amino acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3K81_02470 {ECO:0000313|EMBL:OGD53456.1};
OS Candidatus Bathyarchaeota archaeon RBG_13_60_20.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1797380 {ECO:0000313|EMBL:OGD53456.1, ECO:0000313|Proteomes:UP000177051};
RN [1] {ECO:0000313|EMBL:OGD53456.1, ECO:0000313|Proteomes:UP000177051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGD53456.1}.
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DR EMBL; MEZG01000056; OGD53456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5DES4; -.
DR STRING; 1797380.A3K81_02470; -.
DR Proteomes; UP000177051; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 486 AA; 53625 MW; 334594559CDCA131 CRC64;
MALNNNPGEL TLDPENWAEL RKLGHRMMDD MMDHLEHVRD RPIVQRMPDE AKGAFTQPPP
MQGMGAEAAY RDFVELLLRN QSNFNKHPRF WGFVVGTGSP SGMLADMLAS GLNVNMVGGP
MASTMLEMQV TAWMKGLLGF PAEAGGILVS GGSMANLLGL TVARNAKAEE AKSLGARRGM
TVYGSEEMHV CVQKAVEMLG IGSDNLRKVP VDGDYRINVQ ALEERIREDR AAGLEPFCVV
GNAGTINTGS FDDLEALADL CSREDLWLHV DGAFGAWAAI VPELRHLVRG LDRADSLAFD
LHKWMYMPYD VGCVLFKRQS DQVRTFSNRP DYFAMSKDTP PLFADFGIEL SRSFRALKVW
MGLKENGVSK YQALVKQNVD QARHLKALVE SRPELELMAP VPLNTVCFRY RGQGIPDTAL
DELNRGLSMQ LMFSGAGAAS ETKVNGRVAL RVCITNHRTT RRDLEEFAEA AAKTGAMMAK
TPRSNP
//
