ID   ORTB_ACESD              Reviewed;         469 AA.
AC   E3PY97;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=2-amino-4-ketopentanoate thiolase beta subunit {ECO:0000303|PubMed:4407783};
DE            EC=2.3.1.263 {ECO:0000269|PubMed:4407783};
DE   AltName: Full=AKP thiolase {ECO:0000303|PubMed:4407783};
DE            Short=AKPT {ECO:0000303|PubMed:4407783};
GN   Name=ortB {ECO:0000250|UniProtKB:C1FW07};
GN   OrderedLocusNames=CLOST_1292 {ECO:0000312|EMBL:CBH21412.1};
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND COFACTOR.
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=4407783; DOI=10.1021/bi00711a019;
RA   Jeng I.M., Somack R., Barker H.A.;
RT   "Ornithine degradation in Clostridium sticklandii; pyridoxal phosphate and
RT   coenzyme A dependent thiolytic cleavage of 2-amino-4-ketopentanoate to
RT   alanine and acetyl coenzyme A.";
RL   Biochemistry 13:2898-2903(1974).
CC   -!- FUNCTION: Involved in the ornithine fermentation pathway. Catalyzes the
CC       thiolytic cleavage of 2-amino-4-ketopentanoate (AKP) with coenzyme A
CC       (CoA) to form acetyl-CoA and alanine. It is strictly specific for AKP.
CC       {ECO:0000269|PubMed:4407783}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + D-alanine = (2R)-2-amino-4-oxopentanoate + CoA;
CC         Xref=Rhea:RHEA:51436, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:134102; EC=2.3.1.263;
CC         Evidence={ECO:0000269|PubMed:4407783};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:4407783};
CC   -!- ACTIVITY REGULATION: Completely inhibited by p-chloromercuribenzoate
CC       (p-ClHgBzO) and acetyl-CoA, and partially inhibited by N-
CC       ethylmaleimide. {ECO:0000269|PubMed:4407783}.
CC   -!- SUBUNIT: Heterodimer with OrtA. {ECO:0000250|UniProtKB:C1FW07}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; FP565809; CBH21412.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PY97; -.
DR   SMR; E3PY97; -.
DR   STRING; 1511.CLOST_1292; -.
DR   EnsemblBacteria; CBH21412; CBH21412; CLOST_1292.
DR   KEGG; cst:CLOST_1292; -.
DR   eggNOG; COG0031; Bacteria.
DR   HOGENOM; CLU_577286_0_0_9; -.
DR   OMA; LKCIIVQ; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006591; P:ornithine metabolic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
PE   1: Evidence at protein level;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..469
FT                   /note="2-amino-4-ketopentanoate thiolase beta subunit"
FT                   /id="PRO_0000438121"
FT   BINDING         128
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG59"
FT   BINDING         238..242
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG59"
FT   MOD_RES         102
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG59"
SQ   SEQUENCE   469 AA;  50869 MW;  B4943B71B6A2E901 CRC64;
     MSKDMSYSGV MSRRNEIMKN AIGIDYTTFE SGSLSFDYEK MMRETGYTLE EMQKIQYSTG
     VGRTPVLELR NITALARKYA APGKGARIFI KDEAGNPSGS FKARRAANAV YHAKKLGYKG
     VIAATSGNYG AAVASQAAMA GLKCIIVQEC YDSKGVGQPE IIEKARKCEA LGAEVVQLSV
     GPELFYKFLS LLEETGYFNA SLYTPFGIAG VETLGYELAV EFREAYGKDP DVVVCSNAGG
     GNLTGTARGL IKAGAQSEVV AASVNLQGLH MASDTQFNKK SFTTSHTGFG MPFATWPDRS
     DVPRSAARPL RYMDRYVTVN QGEVFYITET LASLEGLEKG PAGNTALAAA FSLAQEMDKD
     QIIVVQETEY TGAGKHIQPQ LAFARDNGID IKFGNPKEEV AGINIILPEN PGMIKAVDHE
     MNKLRKSLIK NALANYPDAK LDDSDIDFLV KETKSDTEFV KATIKEIKG