ID B9LSA8_HALLT Unreviewed; 403 AA.
AC B9LSA8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN OrderedLocusNames=Hlac_0349 {ECO:0000313|EMBL:ACM55953.1};
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM55953.1, ECO:0000313|Proteomes:UP000000740};
RN [1] {ECO:0000313|EMBL:ACM55953.1, ECO:0000313|Proteomes:UP000000740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC {ECO:0000313|Proteomes:UP000000740};
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
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; CP001365; ACM55953.1; -; Genomic_DNA.
DR RefSeq; WP_012659594.1; NC_012029.1.
DR AlphaFoldDB; B9LSA8; -.
DR GeneID; 7399741; -.
DR KEGG; hla:Hlac_0349; -.
DR eggNOG; arCOG01431; Archaea.
DR HOGENOM; CLU_021152_4_1_2; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000000740; Chromosome 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000000740}.
FT DOMAIN 328..403
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 403 AA; 43027 MW; FB4DFC6FB29D94DB CRC64;
MISLSDVREA RERVGDVARH TPLERSRTFS EMSGADVHLK LENFQRTGAF KIRGAMNRIA
TLSESEREAG VVTASAGNHA QGVALAADRA GVDATVVMPR FAPVSKVKAT RGYGASVRLE
GVDYDEAQAY AHELERKESR TYVHAFDDPV VMAGQGTIGL EIVDDCPDLD TVVVPIGGGG
LISGVAVAIK EQLPDVRVVG VQAEGAASAG ESLKRGEVYE IDSVDTIADG IATRSIGEQT
LEVMSEYVDE VVTVDDREIA LALTLLLERS KTLVEGAGAV ALAAVLSEAF EYENDETIVA
ALCGGNIDLN RLGTVIRRGL VQMGRYLKIT IDLKDRPGEL ERVSSIVART GANVYAVHHD
RTSRDVAVNA AELELELETD DAEHAADIVD ALEADGYVVE VLS
//
