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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//