ILVA_BACSU
ID ILVA_BACSU Reviewed; 422 AA.
AC P37946;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=L-threonine dehydratase biosynthetic IlvA;
DE EC=4.3.1.19;
DE AltName: Full=Threonine deaminase;
GN Name=ilvA; OrderedLocusNames=BSU21770;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Armpriester J.M. Jr., Fink P.S.;
RT "Nucleotide sequence analysis of the Bacillus subtilis 168 ilvA gene.";
RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT artificial chromosomes for sequencing.";
RL Microbiology 142:3005-3015(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and
CC ammonia from threonine in a two-step reaction. The first step involved
CC a dehydration of threonine and a production of enamine intermediates
CC (aminocrotonate), which tautomerizes to its imine form (iminobutyrate).
CC Both intermediates are unstable and short-lived. The second step is the
CC nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-
CC ketobutyrate and free ammonia. In the low water environment of the
CC cell, the second step is accelerated by RidA (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; M58606; AAA22549.1; -; Genomic_DNA.
DR EMBL; L77246; AAA96639.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14095.1; -; Genomic_DNA.
DR PIR; A69644; A69644.
DR RefSeq; NP_390060.1; NC_000964.3.
DR AlphaFoldDB; P37946; -.
DR SMR; P37946; -.
DR IntAct; P37946; 1.
DR MINT; P37946; -.
DR STRING; 224308.BSU21770; -.
DR PaxDb; P37946; -.
DR PRIDE; P37946; -.
DR EnsemblBacteria; CAB14095; CAB14095; BSU_21770.
DR GeneID; 939093; -.
DR KEGG; bsu:BSU21770; -.
DR PATRIC; fig|224308.43.peg.2270; -.
DR eggNOG; COG1171; Bacteria.
DR InParanoid; P37946; -.
DR BioCyc; BSUB:BSU21770-MON; -.
DR SABIO-RK; P37946; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000001570; 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 GO; GO:0006566; P:threonine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR011820; IlvA.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001721; TD_ACT-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR02079; THD1; 1.
DR PROSITE; PS51672; ACT_LIKE; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Isoleucine biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..422
FT /note="L-threonine dehydratase biosynthetic IlvA"
FT /id="PRO_0000185570"
FT DOMAIN 339..413
FT /note="ACT-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT BINDING 87
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 190..194
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 15
FT /note="H -> D (in Ref. 2; AAA96639/CAB14095)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="V -> A (in Ref. 2; AAA96639/CAB14095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46701 MW; 3027A5ED87084140 CRC64;
MKPLLKENSL IQVKHILKAH QNVKDVVIHT PLQRNDRLSE RYECNIYLKR EDLQVVRSFK
LRGAYHKMKQ LSSEQTENGV VCASAGNHAQ GVAFSCKHLG IHGKIFMPST TPRQKVSQVE
LFGKGFIDII LTGDTFDDVY KSAAECCEAE SRTFIHPFDD PDVMAGQGTL AVEILNDIDT
EPHFLFASVG GGGLLSGVGT YLKNVSPDTK VIAVEPAGAA SYFESNKAGH VVTLDKIDKF
VDGAAVKKIG EETFRTLETV VDDILLVPEG KVCTSILELY NECAVVAEPA GALSVAALDL
YKDQIKGKNV VCVVSGGNND IGRMQEMKER SLIFEGLQHY FIVNFPQRAG ALREFLDEVL
GPNDDITRFE YTKKNNKSNG PALVGIELQN KADYGPLIER MNKKPFHYVE VNKDEDLFHL
LI
