ID A0A1H7AZE0_9MICO Unreviewed; 408 AA.
AC A0A1H7AZE0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-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=SAMN05421637_2734 {ECO:0000313|EMBL:SEJ69974.1};
OS Demequina mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Demequinaceae;
OC Demequina.
OX NCBI_TaxID=1043493 {ECO:0000313|EMBL:SEJ69974.1, ECO:0000313|Proteomes:UP000183315};
RN [1] {ECO:0000313|Proteomes:UP000183315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24868 {ECO:0000313|Proteomes:UP000183315};
RA Varghese N.;
RL Submitted (OCT-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 -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004810}.
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DR EMBL; FNZI01000009; SEJ69974.1; -; Genomic_DNA.
DR RefSeq; WP_042215598.1; NZ_FNZI01000009.1.
DR AlphaFoldDB; A0A1H7AZE0; -.
DR STRING; 1043493.SAMN05421637_2734; -.
DR eggNOG; COG1171; Bacteria.
DR OrthoDB; 9811476at2; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000183315; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000183315}.
FT DOMAIN 332..408
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 408 AA; 42235 MW; D71C641BB6A3CBA8 CRC64;
MHEVTLAHVE DAACALAGVA QRTPLDHATY LSELHGCPVS LKLENLQRTG SFKLRGATYR
LSRLTDEERA RGVVAASAGN HAQGVAFAAQ QLGVEATIFM PLGAPVPKLL ATMGYGATVV
TDGATVEECL ALAAAHAERT GAIMIHPFDH ADVIAGQGTI GLEILEDVPD ADTIVVPIGG
GGLIAGVAVA AKAVAAQQGR DIRIVGVQAA ATAAFPPSLA AGHPVTIERG ATIADGIAVV
RPGEHTFPIV RDLVDEVVTV EEDHLARAVL TLLERMKLVV EPAGAAAVAA ILEGLIEPHG
STVALVSGGN IDPLLLQRIV AHGLVASGRY MTIRIPLPDR PGQLARVSEL LAREGANVIE
VLHTRHDQGL TLNDVVLQMS VETRGPNHQT AVIDALRAAG YAPEVVGG
//
