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Database: UniProt
Entry: A0A401V0Z8_9CELL
LinkDB: A0A401V0Z8_9CELL
Original site: A0A401V0Z8_9CELL 
ID   A0A401V0Z8_9CELL        Unreviewed;       398 AA.
AC   A0A401V0Z8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN   ORFNames=CTKZ_21440 {ECO:0000313|EMBL:GCD20582.1};
OS   Cellulomonas algicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=2071633 {ECO:0000313|EMBL:GCD20582.1, ECO:0000313|Proteomes:UP000288246};
RN   [1] {ECO:0000313|EMBL:GCD20582.1, ECO:0000313|Proteomes:UP000288246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKZ-21 {ECO:0000313|EMBL:GCD20582.1,
RC   ECO:0000313|Proteomes:UP000288246};
RA   Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA   Otoguro M., Yanagida F., Hayakawa M.;
RT   "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
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   -!- 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:GCD20582.1}.
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DR   EMBL; BHYL01000168; GCD20582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401V0Z8; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000288246; Unassembled WGS sequence.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
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; 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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51671; ACT; 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:GCD20582.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          324..398
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   398 AA;  41399 MW;  1ADC2A00AC93B860 CRC64;
     MSLDVAAAAR LLDGVAERTP VQRSRAVSQV AGAEVWLKCE NLQRAGSFKI RGAYTRMARL
     TDEERARGVV AASAGNHAQG VALAARILGI EAYVYMPVDA ALPKIAATRD YGAHVELVGT
     SVDEALVHAR EHAERTGAVL VHPFDHPDVV AGQGTIALEI AEQVPDVATV VVPVGGGGLA
     AGVVEALAQV RPDVRVVGVQ AARAAAYPAS LAVHHPVPAL ELRTMADGIA VGLPGGVPFE
     VLDRHHLEVR TVSEEDISRA VLLVAERAKL LVEPSGAVAV AALMAAPGTF EGPVVAILSG
     GNIDPQVLLH VVRHGLASAG RFLALRVRID DRPGALASLL QDIAEAGGNV MHLTHARTGS
     DLAFDQVTVS AQVETKGPEH CAQVMAHLRA TGYQVQGD
//
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