ID A0A3R9SKV8_9ACTN Unreviewed; 409 AA.
AC A0A3R9SKV8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-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=EF917_22290 {ECO:0000313|EMBL:RSR97316.1};
OS Streptomyces sp. WAC00469.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487415 {ECO:0000313|EMBL:RSR97316.1, ECO:0000313|Proteomes:UP000269080};
RN [1] {ECO:0000313|EMBL:RSR97316.1, ECO:0000313|Proteomes:UP000269080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC00469 {ECO:0000313|EMBL:RSR97316.1,
RC ECO:0000313|Proteomes:UP000269080};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivation of ubiquitous gene clusters.";
RL Submitted (NOV-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 -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004810}.
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:RSR97316.1}.
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DR EMBL; RPRX01000090; RSR97316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9SKV8; -.
DR OrthoDB; 9811476at2; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000269080; 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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR045865; ACT-like_dom_sf.
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; SSF55021; ACT-like; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Lyase {ECO:0000313|EMBL:RSR97316.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000269080}.
FT DOMAIN 336..409
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 409 AA; 42184 MW; 5AD4F23FB794F11B CRC64;
MNHGTSGPPS PVTLDDVRGA QKMLSGVARI TPMEGSRHLS RLAGVPVHLK CENLQRTGSF
KLRGAYVRIA GLLPEERAAG VVAASAGNHA QGVALAASLL GVHATVFMPK GAPLPKIGAT
RDYGAEVRLH GQVVDETLAA AQEYADRTGA VFIHPFDHPD IIAGQGTVGL EILEQCPEVG
TVVVGVGGGG LAAGIAVAVK SLRPDVRIVG VQAEGSAAYP PSLASGRPVV IDRPTTMADG
IRVGRPGDVP FGIVRDLVDE VCTVGEDELS AALLLCLERA KLVVEPAGVA PVAALLGGRC
TVRGPAVAVL SGGNVDPVLL QRVLRHGMAA QGRYLAVRLR LTDRPGALAT LLGVVSAADA
NVLDVSHART DPRLGLTEAE VELHLETKGP DHCAEVVRAL RDAGHTVLD
//
