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Database: UniProt
Entry: A0A0F2LEA8_9CREN
LinkDB: A0A0F2LEA8_9CREN
Original site: A0A0F2LEA8_9CREN 
ID   A0A0F2LEA8_9CREN        Unreviewed;       404 AA.
AC   A0A0F2LEA8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN   ORFNames=TU35_01970 {ECO:0000313|EMBL:KJR74091.1};
OS   Thermoproteus sp. AZ2.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=1609232 {ECO:0000313|EMBL:KJR74091.1, ECO:0000313|Proteomes:UP000033636};
RN   [1] {ECO:0000313|EMBL:KJR74091.1, ECO:0000313|Proteomes:UP000033636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Servin-Garciduenas L.E., Martinez-Romero E.;
RT   "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT   Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KJR74091.1}.
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DR   EMBL; JZWT01000012; KJR74091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2LEA8; -.
DR   PATRIC; fig|1609232.3.peg.252; -.
DR   Proteomes; UP000033636; Unassembled WGS sequence.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR   CDD; cd04886; ACT_ThrD-II-like; 1.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR044561; ACT_ThrD-II-like.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR005789; Thr_deHydtase_catblc.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01127; ilvA_1Cterm; 1.
DR   PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:KJR74091.1}.
FT   DOMAIN          329..404
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   404 AA;  43661 MW;  24957FF40B2C69E9 CRC64;
     MEPPLEEALE VIRAQQRSGK IHRTPLLRSE TLSRLTGGDV YLKLEALQKT GSFKIRGAYY
     AMYKYIGEGY RRFITASAGN HAQGVAYAAQ LHGVRATVVM PVTTPWLKVK KTRDYGAEVV
     LAGESYYEAE KKALELAGGS GAKFLHAYND IYVIAGQGTI GVEILEDLAD VDVVVVPVGG
     GGLISGIAYA VKRVRPNAKV IGVQAEGAPG VYLSRKEGKI ITLDKVDTIA DGIAVKRPSE
     LTMEFINKFV DDVVLVDDNE IADAIYLLLE RTRVVAEGAG AASAAALMAG KIDVKGRRAV
     AVVSGGNIDA TMLIRVLNKA MARQRRIAKF VVEVPDRPGT LAAAAAALAS HNINIIDVYH
     ERYDPRQRPN YVEIVFVTEV PGDLDVDAVV KELDARGLKI RHVN
//
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