ID D4GZI8_HALVD Unreviewed; 341 AA.
AC D4GZI8; L9UFD7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:ADE03363.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:ADE03363.1};
GN Name=ltaE {ECO:0000313|EMBL:ADE03363.1};
GN OrderedLocusNames=HVO_0243 {ECO:0000313|EMBL:ADE03363.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE03363.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE03363.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
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}.
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DR EMBL; CP001956; ADE03363.1; -; Genomic_DNA.
DR RefSeq; WP_004045358.1; NZ_AOHU01000107.1.
DR AlphaFoldDB; D4GZI8; -.
DR STRING; 309800.HVO_0243; -.
DR PaxDb; 309800-C498_19474; -.
DR EnsemblBacteria; ADE03363; ADE03363; HVO_0243.
DR GeneID; 8924094; -.
DR KEGG; hvo:HVO_0243; -.
DR PATRIC; fig|309800.29.peg.3794; -.
DR eggNOG; arCOG00113; Archaea.
DR HOGENOM; CLU_029381_0_4_2; -.
DR OrthoDB; 198122at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino 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; 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;
KW Lyase {ECO:0000313|EMBL:ADE03363.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008243}.
FT DOMAIN 3..284
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 341 AA; 35618 MW; B08637F8B69B1912 CRC64;
MIDLRSDTVT LPSDEMREAA RDAAVGDDVY GDDPTVNELE ARAAELVGKE AALFVPSGTM
GNQIAARVHA DPGQEALVDE KAHVYEWEVG GFAQLSGLQV RAYDAGERAA PTPAQVRDHA
REESLHVAGT GVLCLENTHN ARGGVAVPKA DIDAAADAAR DLGIPVHLDG ARLFNACVAL
DEDPTAMVER VDTVMCCLSK GLGAPVGSML AGPEAFIEEA VRVRKQFGGG MRQAGLIAAP
GLVALDNVDR LADDHANATV LAEGLDAVSG LSVPTPDTNI VVVDSEGAGL TAEEFVELCD
DVGVLGGTFG QYHTRFTTNL NVSRADVERA VDLVADAVES R
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