ID A2BJD5_HYPBU Unreviewed; 368 AA.
AC A2BJD5;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Decarboxylase {ECO:0000313|EMBL:ABM80096.1};
GN OrderedLocusNames=Hbut_0224 {ECO:0000313|EMBL:ABM80096.1};
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM80096.1, ECO:0000313|Proteomes:UP000002593};
RN [1] {ECO:0000313|EMBL:ABM80096.1, ECO:0000313|Proteomes:UP000002593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC {ECO:0000313|Proteomes:UP000002593};
RX PubMed=17350933;
RA Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
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. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR EMBL; CP000493; ABM80096.1; -; Genomic_DNA.
DR RefSeq; WP_011821413.1; NC_008818.1.
DR AlphaFoldDB; A2BJD5; -.
DR STRING; 415426.Hbut_0224; -.
DR EnsemblBacteria; ABM80096; ABM80096; Hbut_0224.
DR GeneID; 4782395; -.
DR KEGG; hbu:Hbut_0224; -.
DR eggNOG; arCOG00027; Archaea.
DR HOGENOM; CLU_751445_0_0_2; -.
DR OrthoDB; 56891at2157; -.
DR Proteomes; UP000002593; Chromosome.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002593}.
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 368 AA; 39554 MW; 6305813390473769 CRC64;
MEWLRGGSWE EVARELGELR AGEPSPCRVA GSTVAEPLPV ARRAYSLYAD VNLNDPASWP
SVTKLLEGIS RVLEELRLGH RWLVAVSGGS EAVLTGLYIA REYTRGRVVV ASSAAHASVL
KAARVLGMEV KLVQVDSRLR IDLYALEKTL RGVQNVAAIV ATAGVTDNGA VDPVRDVAKL
AWEHGAVVYV DAAFGGLPLL GLGSTETVLP RGGPALAGID FHKHVAPPPS SILVSNTAEL
RDYIVFPAPY MPLGRQETLL WTRPASGLAA AYAALRALGA SGVGELARYL YRLASKLASI
LEQRGVELLS PLDTPLVAFR PPSVEGALKR LRRRGWILYP SRLPGILRYV AKWCHEPGDV
EEIAEAVA
//
