ID A0A1S2I7A6_9MICO Unreviewed; 414 AA.
AC A0A1S2I7A6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN ORFNames=BIV00_03950 {ECO:0000313|EMBL:OII20688.1};
OS Curtobacterium sp. MCBA15_012.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1898738 {ECO:0000313|EMBL:OII20688.1};
RN [1] {ECO:0000313|EMBL:OII20688.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBA15_012 {ECO:0000313|EMBL:OII20688.1};
RA Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT "Evidence for ecological flexibility in the cosmopolitan genus
RT Curtobacterium.";
RL Submitted (SEP-2016) 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:OII20688.1}.
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DR EMBL; MJGP01000004; OII20688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S2I7A6; -.
DR STRING; 1898738.BIV00_03950; -.
DR OrthoDB; 9811476at2; -.
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:OII20688.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 338..414
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 414 AA; 43306 MW; 52F045EE8D362C56 CRC64;
MPQQQTAAFP TLADIEAARR TIAGVARVTP METSEFLAGL LGSPVHLKCE NLQRTGAYKL
RGAYNRLAAL SPEERAAGVV AASAGNHAQG VALAARELGI PATIFTPVGV ALPKLQATRH
YGAEVVLRGH SVEEALSAAK EFSNRTGAVF IPPFDHPAVI AGQGTLGLEI LDQVPDVDTV
VVPIGGGGVI SGIALAVKGT AERLGREIRV IGVQAENAAA YPSSISAGEP VTVTTRPTIA
DGIAVARPGD MNFPIIRDHV DEIVTVSDDD TARALLVLLE RAKLVVEAAG AVGVAAIMSG
AVRDTGRTVV LLSGGNIDPL MMERVITRGL VAASRYIGIR IMLPDRPGQL ARVAQVISDA
GANVVEVLHT RHGQGLVINE VALDLSIEAR GPEHAQEVMQ RLHEVGFQPE LLEH
//
