ID Q7VC15_PROMA Unreviewed; 513 AA.
AC Q7VC15;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=L-threonine dehydratase {ECO:0000256|RuleBase:RU362012};
DE EC=4.3.1.19 {ECO:0000256|RuleBase:RU362012};
DE AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU362012};
GN Name=ilvA {ECO:0000256|RuleBase:RU362012,
GN ECO:0000313|EMBL:AAP99971.1};
GN OrderedLocusNames=Pro_0927 {ECO:0000313|EMBL:AAP99971.1};
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167539 {ECO:0000313|EMBL:AAP99971.1, ECO:0000313|Proteomes:UP000001420};
RN [1] {ECO:0000313|EMBL:AAP99971.1, ECO:0000313|Proteomes:UP000001420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420};
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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.
CC {ECO:0000256|ARBA:ARBA00025527, ECO:0000256|RuleBase:RU362012}.
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:0000256|ARBA:ARBA00001274,
CC ECO:0000256|RuleBase:RU362012};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362012};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004810, ECO:0000256|RuleBase:RU362012}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU362012}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000256|ARBA:ARBA00010869, ECO:0000256|RuleBase:RU362012}.
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DR EMBL; AE017126; AAP99971.1; -; Genomic_DNA.
DR RefSeq; NP_875319.1; NC_005042.1.
DR RefSeq; WP_011125079.1; NC_005042.1.
DR AlphaFoldDB; Q7VC15; -.
DR STRING; 167539.Pro_0927; -.
DR EnsemblBacteria; AAP99971; AAP99971; Pro_0927.
DR KEGG; pma:Pro_0927; -.
DR PATRIC; fig|167539.5.peg.975; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_6_0_3; -.
DR OrthoDB; 9811476at2; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000001420; Chromosome.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04906; ACT_ThrD-I_1; 1.
DR CDD; cd04907; ACT_ThrD-I_2; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001721; TD_ACT-like.
DR InterPro; IPR038110; TD_ACT-like_sf.
DR InterPro; IPR005787; Thr_deHydtase_biosynth.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01124; ilvA_2Cterm; 1.
DR PANTHER; PTHR48078:SF11; THREONINE DEHYDRATASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 2.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51672; ACT_LIKE; 2.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU362012};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624,
KW ECO:0000256|RuleBase:RU362012}; Lyase {ECO:0000256|RuleBase:RU362012};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362012};
KW Reference proteome {ECO:0000313|Proteomes:UP000001420};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 328..399
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
FT DOMAIN 429..500
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
SQ SEQUENCE 513 AA; 57653 MW; F8B6EEF089851C2E CRC64;
MVDYLHKILT ARVYDVARET PLEKAFNLSK RVQNDIWLKR EDLQPVFSFK LRGAYNRMSN
LTQKELEKGV VASSAGNHAQ GVALSAQHLK CRAVIVMPIT TPPVKIQAVK SLKAKVILHG
DTYDEAYLEA IRLSKEEELV FIHPFDDPLV IAGQGTIGVE ILRQIDQPPY AIYVAVGGGG
LIAGVGAYIK NLWPEVKIIG VEPEDASAMT SSLKANKRIE LSNVGLFADG VAVKQVGEET
FKLAKKYVDE MITVNTDQIC AAIKDFFEDT RGILEPAGAL AIAGLKAHIQ KNDLKDKHLV
AITCGANMNF ERLRFVAERA LLGESKEAMM AIEIEEKAGS LKMLCKVIDN RNLTEFSYRI
SQTKTANIFM AVEVANKEDR ISLFNKIKSH GFKIIDLSDD ELSKIHLRHM IGGRFPNVIR
NQKKSYKELL YRFEFPERPG ALMNFLEAMN PEWSISIFNY RNHGADIGRI VIGVLVHDKD
LVAWRNFLNE LGYKYWEETE NAAYKLFLGA QHE
//
