ID M0NC93_9EURY Unreviewed; 336 AA.
AC M0NC93;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:EMA55193.1};
GN ORFNames=C450_03982 {ECO:0000313|EMBL:EMA55193.1};
OS Halococcus salifodinae DSM 8989.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227456 {ECO:0000313|EMBL:EMA55193.1, ECO:0000313|Proteomes:UP000011625};
RN [1] {ECO:0000313|EMBL:EMA55193.1, ECO:0000313|Proteomes:UP000011625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8989 {ECO:0000313|EMBL:EMA55193.1,
RC ECO:0000313|Proteomes:UP000011625};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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:EMA55193.1}.
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DR EMBL; AOME01000015; EMA55193.1; -; Genomic_DNA.
DR RefSeq; WP_005040254.1; NZ_AOME01000015.1.
DR AlphaFoldDB; M0NC93; -.
DR STRING; 1227456.C450_03982; -.
DR PATRIC; fig|1227456.3.peg.825; -.
DR OrthoDB; 198122at2157; -.
DR Proteomes; UP000011625; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd06502; TA_like; 1.
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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041359; GntG_guanitoxin; 1.
DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
FT DOMAIN 3..285
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 336 AA; 35926 MW; FDB993193C278642 CRC64;
MIDLRSDTVT RPSDEMRVAA SEADVGDDVY REDPTVNELE AEAAAAVGME AALYVPTGTM
GNQVAARTHT DRGEELLCER ESHVYKWEVG GLAQLSGLQP RTVDGGSRGT ITPSDIHEGY
VEEDTHRPGT GLLCLENTHN SKGGVAIAPE EIDAAADAAH ELDIPVHVDG ARVFNAAVAH
DVDASRVVRE VDSVMFCLSK GLGAPVGSML AGSEAFIERA RRHRKLFGGG MRQAGIIAAP
GLEALSNVDR LAEDHENAAV LAEGLDDIDG LAVQSPETNI VLVETEPTAE EFLERVADEG
VQGTAFGEHV VRFCTHLDID RSDVERAVED VRRAMT
//
