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Database: UniProt
Entry: D5BR72_PUNMI
LinkDB: D5BR72_PUNMI
Original site: D5BR72_PUNMI 
ID   D5BR72_PUNMI            Unreviewed;       406 AA.
AC   D5BR72;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=L-serine dehydratase {ECO:0000256|ARBA:ARBA00031418};
DE            EC=4.3.1.17 {ECO:0000256|ARBA:ARBA00012093};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN   OrderedLocusNames=SAR116_0526 {ECO:0000313|EMBL:ADE38769.1};
OS   Puniceispirillum marinum (strain IMCC1322).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC   Puniceispirillum.
OX   NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE38769.1, ECO:0000313|Proteomes:UP000007460};
RN   [1] {ECO:0000313|EMBL:ADE38769.1, ECO:0000313|Proteomes:UP000007460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE38769.1,
RC   ECO:0000313|Proteomes:UP000007460};
RX   PubMed=20382761; DOI=10.1128/JB.00347-10;
RA   Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.;
RT   "Complete genome sequence of "Candidatus Puniceispirillum marinum"
RT   IMCC1322, a representative of the SAR116 clade in the
RT   Alphaproteobacteria.";
RL   J. Bacteriol. 192:3240-3241(2010).
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. TdcB also dehydrates
CC       serine to yield pyruvate via analogous enamine/imine intermediates.
CC       {ECO:0000256|ARBA:ARBA00025594}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004810}.
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DR   EMBL; CP001751; ADE38769.1; -; Genomic_DNA.
DR   RefSeq; WP_013045398.1; NC_014010.1.
DR   AlphaFoldDB; D5BR72; -.
DR   STRING; 488538.SAR116_0526; -.
DR   KEGG; apb:SAR116_0526; -.
DR   eggNOG; COG1171; Bacteria.
DR   eggNOG; COG2061; Bacteria.
DR   HOGENOM; CLU_021152_4_1_5; -.
DR   OrthoDB; 9811476at2; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000007460; Chromosome.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC.
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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; 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.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 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:ADE38769.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007460}.
FT   DOMAIN          326..405
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   406 AA;  43711 MW;  20B171AB63B17FFF CRC64;
     MGVSAQDIRD AATLLDGNVI RTPMIKSPLL SRHLGCEVYV KLECQQYTSS FKARGAYVAM
     LGLDDKQREK GVIAMSAGNH AQAVAYHAEA MGIPAVIVMP SQTPFAKVTR TRSYGAEVVL
     EGRNLNECEN TVQKLIEERG LTLIHPYDNE KVMQGQGTVG LEMLEDQPDL DMLVVPIGGG
     GLMGGISTIA RDMRPDLKIY GVQTEAYPSM KLAVAGQEIV CGGETLAEGI AVKKPGGVTL
     PAIEKNVDDI LLVNEQQLEW AVGALIEQQR VVSEGAGAAG IAALYAYPEM FAGQKVGVVI
     CGGNIDPRLL ASILNRNMAS DGRVARLRID ISDEPGMLAA ITASIGRCGG NIIEIYHQRL
     FFDVPAKLAK IDAVIETRGT EHVKEIIDDL RKANFTVRQL DDADKN
//
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