ID Q82I56_STRAW Unreviewed; 409 AA.
AC Q82I56;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN Name=ilvA {ECO:0000313|EMBL:BAC71013.1};
GN ORFNames=SAVERM_3302 {ECO:0000313|EMBL:BAC71013.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC71013.1, ECO:0000313|Proteomes:UP000000428};
RN [1] {ECO:0000313|EMBL:BAC71013.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2] {ECO:0000313|EMBL:BAC71013.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; BA000030; BAC71013.1; -; Genomic_DNA.
DR RefSeq; WP_010984732.1; NZ_JZJK01000090.1.
DR AlphaFoldDB; Q82I56; -.
DR KEGG; sma:SAVERM_3302; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_1_11; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000000428; Chromosome.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000000428}.
FT DOMAIN 336..409
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 409 AA; 42431 MW; 4E3F81DCCC948407 CRC64;
MSYSTADSLP AVTLDDVRGA QKMLAGVARM TGMEGSRHLS QLVGAPVHFK CENLQRTGSF
KLRGAYVRIA GLLPEERAAG VVAASAGNHA QGVALASSLL GVRSTVFMPK AAPLPKISAT
REYGAEVRLH GTVVDETLAA AQEYAAETGA VFIHPFDHPD IIAGQGTVGL EILEQCPEVR
TIVVGIGGGG LAAGIATAVK ALRPDVRIVG VQAAGAAAYP PSLAAGRPVS VENPATMADG
IKVGRPGDVP FRIIGDLVDE VRTVSEGNLS SALLLCLERA KLVVEPAGAS PVAALLREPG
AFEGPVVAVL SGGNVDPLLM QRILRHGMAA AGRYLAVRLR LTDRPGALAT LLGVLPTVDA
NVLDVSHVRT DPRLGLTEVE VELHLETKGP EHCAEVEQAL REAGYTVID
//
