ID   ORTA_ACESD              Reviewed;         101 AA.
AC   E3PY98;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=2-amino-4-ketopentanoate thiolase alpha 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=ortA {ECO:0000250|UniProtKB:C1FW06};
GN   OrderedLocusNames=CLOST_1293 {ECO:0000312|EMBL:CBH21413.1};
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, AND ACTIVITY REGULATION.
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   -!- 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 OrtB. {ECO:0000250|UniProtKB:C1FW06}.
CC   -!- SIMILARITY: Belongs to the OrtA family. {ECO:0000305}.
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DR   EMBL; FP565809; CBH21413.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PY98; -.
DR   STRING; 1511.CLOST_1293; -.
DR   EnsemblBacteria; CBH21413; CBH21413; CLOST_1293.
DR   KEGG; cst:CLOST_1293; -.
DR   eggNOG; ENOG503315M; Bacteria.
DR   HOGENOM; CLU_2286677_0_0_9; -.
DR   OMA; KYEHDFG; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006591; P:ornithine metabolic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..101
FT                   /note="2-amino-4-ketopentanoate thiolase alpha subunit"
FT                   /id="PRO_0000438118"
SQ   SEQUENCE   101 AA;  11569 MW;  0567438FE2127A93 CRC64;
     MAKKGDWVLI HKIVLSPEER APQVPDDTKK VPLEMWIKGY LNEDAQIGDQ VSITTRTKRV
     EEGKLLEVNP YYTHDFGKFV PELLKISEQV REITFGGEGN E