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Database: UniProt
Entry: A0A498GB36_9EURY
LinkDB: A0A498GB36_9EURY
Original site: A0A498GB36_9EURY 
ID   A0A498GB36_9EURY        Unreviewed;       403 AA.
AC   A0A498GB36;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN   ORFNames=D3D02_05330 {ECO:0000313|EMBL:RLM90193.1};
OS   Halobellus sp. Atlit-38R.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halobellus.
OX   NCBI_TaxID=2282131 {ECO:0000313|EMBL:RLM90193.1, ECO:0000313|Proteomes:UP000277703};
RN   [1] {ECO:0000313|EMBL:RLM90193.1, ECO:0000313|Proteomes:UP000277703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Atlit-38R {ECO:0000313|EMBL:RLM90193.1,
RC   ECO:0000313|Proteomes:UP000277703};
RA   Turgeman-Grott I.;
RT   "Pervasive acquisition of CRISPR memory from multiple replicons driven by
RT   inter-species mating of archaea.";
RL   Submitted (SEP-2018) 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:RLM90193.1}.
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DR   EMBL; QXIJ01000003; RLM90193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498GB36; -.
DR   OrthoDB; 9915at2157; -.
DR   Proteomes; UP000277703; 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; PF13291; ACT_4; 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:RLM90193.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277703}.
FT   DOMAIN          328..403
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   403 AA;  43252 MW;  21DC62123083654A CRC64;
     MLSLADVEAA RDRIEDIARW TPLEYSHTFS DMTGADVHLK LETFQRTGAF KIRGATNRIA
     TLSAAEREAG VVTASAGNHA QGVALAASRS GVDSKIVMPE HAPISKVEAT ERYGGQTVLY
     GADYDEAQAK AHEIEREEGR TYVHAFNDEV VMAGQGTIGL EIVDDCPEVD TVVVPIGGGG
     LISGIATAVT GRKPDARVIG VQAEGAASLP QSLQAGEIRE LDAVNTIADG IATRKVGERP
     FEVIQERVDE VVTVSDEEIA VALTYLLERE KTLVEGAGAV PLAALLFEAF DYEDGETIVP
     ALCGGNIDTN QLTTVLVRGL VETGRYLKIR TVLRDRPGAL QDLVEIISDQ RANIYAIQHD
     RTSRDVAMNE ADVEIDIETR GHDHIEELLA ALRAAGYSVD VLA
//
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