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Database: UniProt
Entry: D7FWM2_ECTSI
LinkDB: D7FWM2_ECTSI
Original site: D7FWM2_ECTSI 
ID   D7FWM2_ECTSI            Unreviewed;       471 AA.
AC   D7FWM2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:CBJ32110.1};
GN   Name=THA2 {ECO:0000313|EMBL:CBJ32110.1};
GN   ORFNames=Esi_0308_0036 {ECO:0000313|EMBL:CBJ32110.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ32110.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBJ32110.1, ECO:0000313|Proteomes:UP000002630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX   PubMed=20520714; DOI=10.1038/nature09016;
RA   Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA   Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA   Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA   Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA   Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA   Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA   Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA   Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA   Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA   Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA   Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA   Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA   Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of multicellularity in
RT   brown algae.";
RL   Nature 465:617-621(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; FN648496; CBJ32110.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7FWM2; -.
DR   STRING; 2880.D7FWM2; -.
DR   EnsemblProtists; CBJ32110; CBJ32110; Esi_0308_0036.
DR   eggNOG; KOG1368; Eukaryota.
DR   InParanoid; D7FWM2; -.
DR   OMA; MRQTGFM; -.
DR   OrthoDB; 178754at2759; -.
DR   Proteomes; UP000002630; Chromosome LG23.
DR   GO; GO:0016829; F:lyase activity; 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; 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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT   DOMAIN          126..410
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   REGION          39..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  48820 MW;  457765B48255B8A7 CRC64;
     MRGQAMHMLA SSPVVARGIP NGAAPHASRR RFASLLLGTE GRHPSHGSSG SNSSNRTDNS
     NAESGYVAGA SPAGIPAPLW HQKGQLQQLT TVTVTNHEAP AKSSSSSSSS DSTAGASRAA
     PTAAVDLRSD TMTKPCKRLR AAMAGAEVGD DVFGEDPTVV RLEDCVAYLL GKEKGLLVPS
     GTMGNLIAVG AHCRRGDELI LGDKSHIFQY EGAGASALMG VSYHTVRNAE DGGLEVADIQ
     TAVRGDDPHY PRSSLLCLEN TQNLCGARAI AASRMAEMCA AGRHAGLKVH VDGARLWNAA
     VSLEVRPSEL VSDADSVSVC LSKGLGAPVG SVLVGSEQFI YEARRLRKSL GGGMRQSGVI
     AAAGLEAVVN NYVRLSEDHD NAAALASGLG ALRGISAERS PGDTNAVYFQ VTGMDAQAFV
     DALERDHGVL MGSGYFGGST IRAMTHLDVN REGVERAIEA SRAVLAEAPA S
//
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