ID B0RH37_CLAMS Unreviewed; 458 AA.
AC B0RH37;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN OrderedLocusNames=CMS2433 {ECO:0000313|EMBL:CAQ02513.1};
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ02513.1, ECO:0000313|Proteomes:UP000001318};
RN [1] {ECO:0000313|EMBL:CAQ02513.1, ECO:0000313|Proteomes:UP000001318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC {ECO:0000313|Proteomes:UP000001318};
RX PubMed=18192393; DOI=10.1128/JB.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; AM849034; CAQ02513.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RH37; -.
DR STRING; 31964.CMS2433; -.
DR KEGG; cms:CMS2433; -.
DR eggNOG; COG1171; Bacteria.
DR eggNOG; COG2061; Bacteria.
DR HOGENOM; CLU_021152_4_1_11; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000001318; 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; 3.30.70.260; -; 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; PF01842; ACT; 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}.
FT DOMAIN 382..458
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 48252 MW; 3C6360319CEF5D42 CRC64;
MTDAAPARTP AEEAAAAPHA DLPHLRAVGD ELDPSQLGEE AAALAQELPR GSAPTLARIE
AAREVVSRVA EVTPMESSRF LAEILGSPVH LKCENLQRTG SYKIRGAYNR ISRLTDEEKA
RGVVAASAGN HAQGVAFAAR ELGIRATIFM PVGVALPKLQ ATRQYGAEVI LRGHTVAEPL
LAAAEFAAQT GAVLIPPFDH VDVITGQATL GLEILDQTPA VETVVVPIGG GGLISGVATA
LKLRAAEEGR TIRVVGVQAR NAAAYPPSLA AGRATEIEIT PTIADGIAVA KPGLLNFDII
RDSVDEVVTV EDDDTARALL LLLERAKLVV EPAGAVGVAA ILAGLVEDAG RTVVILSGGN
IDPLMMERVI SRGLAASDRY VKLRIMLPDR PGQLARTSQI ISEANANVVE VLHTRHGRGL
QISEVELEVS VETRGPEHTG EVVQRLRDAG YDPRLQRD
//
