ID U3TBG8_9CREN Unreviewed; 459 AA.
AC U3TBG8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:BAN90887.1};
GN ORFNames=ACAM_1418 {ECO:0000313|EMBL:BAN90887.1};
OS Aeropyrum camini SY1 = JCM 12091.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=1198449 {ECO:0000313|EMBL:BAN90887.1, ECO:0000313|Proteomes:UP000016887};
RN [1] {ECO:0000313|EMBL:BAN90887.1, ECO:0000313|Proteomes:UP000016887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY1 {ECO:0000313|EMBL:BAN90887.1,
RC ECO:0000313|Proteomes:UP000016887};
RX PubMed=23872576; DOI=10.1128/AEM.01089-13;
RA Daifuku T., Yoshida T., Kitamura T., Kawaichi S., Inoue T., Nomura K.,
RA Yoshida Y., Kuno S., Sako Y.;
RT "Variation of the Virus-Related Elements within Syntenic Genomes of the
RT Hyperthermophilic Archaeon Aeropyrum.";
RL Appl. Environ. Microbiol. 79:5891-5898(2013).
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; AP012489; BAN90887.1; -; Genomic_DNA.
DR RefSeq; WP_022542155.1; NZ_BBBZ01000002.1.
DR AlphaFoldDB; U3TBG8; -.
DR STRING; 1198449.ACAM_1418; -.
DR GeneID; 17110651; -.
DR KEGG; acj:ACAM_1418; -.
DR PATRIC; fig|1198449.6.peg.1432; -.
DR eggNOG; arCOG00027; Archaea.
DR OrthoDB; 56891at2157; -.
DR Proteomes; UP000016887; 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}.
FT MOD_RES 238
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 459 AA; 49889 MW; D48C199F48B987DB CRC64;
MSGGRVEEVV KRLAEIRAMD ARGEGGRLFT YLYETGDPGV KEVSLRAFEM FLDTNALDPT
VFKSALFFER ELVSFASSLA GGVEGVVGTV TYGGTESIIL AAMAAREWYR SLGGSRTPGI
VAPQTVHPSV RKAASYLGMR LSIAPVDPGS KRVDIDRLAS LVDDGTAMVV VSAPNYPYGT
VDDVRGVAEA LSGRRVWLHV DACIGGFILP FMRELGLYNG AFAFDVEGVY SVSMDLHKYG
YSPKGASVLL FRDGSLKKHS IFADLRWPGY PFINATVLSS RSVAPLAAAW AVANYLGRRG
YLELARKAVE ARDEIMRGLE SIGFRSIAPI ESTILSVALD DPVDTLRFHA NMSRRGWILG
LQPGVKGLAP PNIHLTISPI HKLVTPQFLR DARASSGEPL PEELEEARHL LESRGPLELA
GMIGRTPYDQ VIIAWILSSI PPDVAEDLAR ELTVEVYHG
//
