TSAL_GEOSL
ID TSAL_GEOSL Reviewed; 402 AA.
AC Q74FW6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=L-threonine ammonia-lyase {ECO:0000303|PubMed:18245290};
DE EC=4.3.1.19 {ECO:0000269|PubMed:18245290};
DE AltName: Full=L-serine ammonia-lyase {ECO:0000303|PubMed:18245290};
DE EC=4.3.1.17 {ECO:0000269|PubMed:18245290};
DE AltName: Full=Threonine/serine ammonia-lyase {ECO:0000303|PubMed:18245290};
GN Name=tdcB {ECO:0000303|PubMed:18245290, ECO:0000312|EMBL:AAR33818.1};
GN OrderedLocusNames=GSU0486 {ECO:0000312|EMBL:AAR33818.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=18245290; DOI=10.1128/jb.01841-07;
RA Risso C., Van Dien S.J., Orloff A., Lovley D.R., Coppi M.V.;
RT "Elucidation of an alternate isoleucine biosynthesis pathway in Geobacter
RT sulfurreducens.";
RL J. Bacteriol. 190:2266-2274(2008).
CC -!- FUNCTION: Catalyzes the conversion of threonine to 2-oxobutanoate and
CC ammonia. Functions in the threonine-dependent pathway of isoleucine
CC biosynthesis, which is the minor pathway for isoleucine biosynthesis in
CC G.sulfurreducens. Also displays serine ammonia-lyase activity, yielding
CC pyruvate from L-serine. {ECO:0000269|PubMed:18245290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC Evidence={ECO:0000269|PubMed:18245290};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC Evidence={ECO:0000269|PubMed:18245290};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P04968};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1. {ECO:0000269|PubMed:18245290}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show undetectable
CC threonine ammonia-lyase and serine ammonia-lyase activities. They are
CC capable of growth in the absence of isoleucine, whereas mutants lacking
CC both tdcB and the citramalate synthase cimA are auxotrophs for
CC isoleucine. {ECO:0000269|PubMed:18245290}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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; AE017180; AAR33818.1; -; Genomic_DNA.
DR RefSeq; NP_951545.1; NC_002939.5.
DR RefSeq; WP_010941154.1; NC_002939.5.
DR AlphaFoldDB; Q74FW6; -.
DR SMR; Q74FW6; -.
DR STRING; 243231.GSU0486; -.
DR EnsemblBacteria; AAR33818; AAR33818; GSU0486.
DR KEGG; gsu:GSU0486; -.
DR PATRIC; fig|243231.5.peg.485; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_1_7; -.
DR InParanoid; Q74FW6; -.
DR OMA; LIHPFDH; -.
DR BRENDA; 4.3.1.19; 7676.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR CDD; cd04886; ACT_ThrD-II-like; 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; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR01127; ilvA_1Cterm; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Isoleucine biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..402
FT /note="L-threonine ammonia-lyase"
FT /id="PRO_0000430580"
FT DOMAIN 327..402
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT BINDING 78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT BINDING 178..181
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT BINDING 302
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04968"
SQ SEQUENCE 402 AA; 43198 MW; C63B20FE3C888D54 CRC64;
MLPYTLIQEA DDRLRKRVRR TELIHSHHFS EKLGIPIYFK CENLQRTGAF KIRGALNFMT
SQPREALAKG VITASAGNHA QGVAFSADLL GVPSTVFMPE STPPQKVFAT RDYGAEVVLT
GRNFDEAYAA AVQAQEERGA LFVHPFDDPL VMAGQGTIGL EVLQELPDVA NILVPIGGGG
LIAGIATAIR ETHPHVRIIG VETAAAPSAH YSLQKGKIVQ VPVTVTLADG IAVKKPGVNT
FPIIRDLVDE VVLVEEEEIA LAIVALLERT KLLVEGAGAV PLAALLNRRV TDLSGKTVCV
LSGGNIDVKT ISVVVERGLV AAGRYLKLKV ELDDLPGALA RLATEIAEAK ANISIITHDR
RSKSLPIGKT EVLIELETRG FEHIQEVISH LQGVGYLVDV LK
