ID A0A0S9RAQ6_9ACTN Unreviewed; 397 AA.
AC A0A0S9RAQ6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN ORFNames=ASF37_10355 {ECO:0000313|EMBL:KQP79162.1};
OS Aeromicrobium sp. Leaf289.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP79162.1, ECO:0000313|Proteomes:UP000051640};
RN [1] {ECO:0000313|Proteomes:UP000051640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQP79162.1}.
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DR EMBL; LMNK01000002; KQP79162.1; -; Genomic_DNA.
DR RefSeq; WP_056580580.1; NZ_LMNK01000002.1.
DR AlphaFoldDB; A0A0S9RAQ6; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000051640; 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:KQP79162.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000051640}.
FT DOMAIN 325..397
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 397 AA; 41542 MW; D29A6F9DBAE0549F CRC64;
MVDLRDVEAA RELIAPVVER TPMAHSRWLS QRVGTDVHLK CENLQRTGSF KIRGAYVRIA
RLSDAERARG VVAASAGNHA QGVALAAQLL GAKATIFMPD GAALPKIAAT RGYGADIEFA
GTGVTEALVH AQEFAERTGA VLIHPFDHAD VLAGQGTVGL EIIEQLPDVR TVLVPLGGGG
LAAGIALLRE RRPDVSVVGV QAADAAAYPT SLAEGHPVTG VMGPTMADGI AVAQPGLIPF
EVIAEQLDDV VTVSEDAMSA ALIGLLERAK MLVEPSGAAG VAALLDDPGR FQGPVVPVLS
GGNIDALLLL DVIRHGLSAA GRFMQLRVRF SDRPGELMRL LTDLADLQVN VLDVAHDRSA
ESLGVREVEV AVQAATRGPD HAEASRRRLG ELGHLLV
//
