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Database: UniProt
Entry: A0A2T0V494_9MICO
LinkDB: A0A2T0V494_9MICO
Original site: A0A2T0V494_9MICO 
ID   A0A2T0V494_9MICO        Unreviewed;       422 AA.
AC   A0A2T0V494;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN   ORFNames=B0I08_1119 {ECO:0000313|EMBL:PRY64992.1};
OS   Glaciihabitans tibetensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Glaciihabitans.
OX   NCBI_TaxID=1266600 {ECO:0000313|EMBL:PRY64992.1, ECO:0000313|Proteomes:UP000237983};
RN   [1] {ECO:0000313|EMBL:PRY64992.1, ECO:0000313|Proteomes:UP000237983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12484 {ECO:0000313|EMBL:PRY64992.1,
RC   ECO:0000313|Proteomes:UP000237983};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-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:PRY64992.1}.
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DR   EMBL; PVTL01000011; PRY64992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0V494; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000237983; 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; 3.40.50.1100; -; 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; 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:PRY64992.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237983}.
FT   DOMAIN          347..422
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   422 AA;  43944 MW;  FF9B4FB54AC6BC5E CRC64;
     MNDTITASSA APAPAVAGPT LEDFEAARAT VGAVADITPL ESSRFLAEVL GSPVYLKCEN
     LQRTGSYKIR GAYNRLAGLS EEDRARGVVA ASAGNHAQGV AFAARELGIK STIFMPIGVA
     LPKLQATRGY GADVVLRGHT VAEPLLAAAE FATETGAIFI PPFDHADVVA GQGTLGLEIL
     DQLPETDTII VPIGGGGLIS GVASAAKQKA ALLGRTIRVI GVQAANAAPY PLSLTMGEPT
     TITIIPTIAD GIAVARPGVL NFEIVRDTVD EIVTVEEDDI ARALLVLLER AKLVVEPAGA
     VAVAAILAGK ITPTGNTVAI LSGGNIDPLV MERIISHGLA ASERYLKLRI PLPDRPGQLA
     RTAEVVAESN ANVVEVLHSR HGSGMQISMV ELELHIETRG PEHADLVLHN LREAGFAPRV
     DF
//
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