ID   ORTA_UNKP               Reviewed;         101 AA.
AC   C1FW06;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=2-amino-4-ketopentanoate thiolase alpha subunit {ECO:0000303|PubMed:19251850};
DE            EC=2.3.1.263 {ECO:0000305|PubMed:19251850};
DE   AltName: Full=AKP thiolase {ECO:0000303|PubMed:19251850};
DE            Short=AKPT {ECO:0000303|PubMed:19251850};
GN   Name=ortA {ECO:0000303|PubMed:19251850};
GN   ORFNames=DIG-28672_34 {ECO:0000312|EMBL:CAQ42979.1};
OS   Unknown prokaryotic organism.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=2725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   Genoscope - CEA;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX   PubMed=19251850; DOI=10.1128/jb.01777-08;
RA   Fonknechten N., Perret A., Perchat N., Tricot S., Lechaplais C.,
RA   Vallenet D., Vergne C., Zaparucha A., Le Paslier D., Weissenbach J.,
RA   Salanoubat M.;
RT   "A conserved gene cluster rules anaerobic oxidative degradation of L-
RT   ornithine.";
RL   J. Bacteriol. 191:3162-3167(2009).
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:19251850}.
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:0000305|PubMed:19251850};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=18 uM for CoA {ECO:0000269|PubMed:19251850};
CC         KM=35 uM for AKP {ECO:0000269|PubMed:19251850};
CC         Note=kcat is 3.5 sec(-1) for CoA as substrate. kcat is 3.4 sec(-1)
CC         for AKP as substrate. {ECO:0000269|PubMed:19251850};
CC   -!- SUBUNIT: Heterodimer with OrtB. {ECO:0000269|PubMed:19251850}.
CC   -!- SIMILARITY: Belongs to the OrtA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU695247; CAQ42979.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1FW06; -.
DR   KEGG; ag:CAQ42979; -.
DR   BioCyc; MetaCyc:AKPTHIOLST-MON; -.
DR   BRENDA; 2.3.1.263; 1522.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006591; P:ornithine metabolic process; TAS:UniProtKB.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..101
FT                   /note="2-amino-4-ketopentanoate thiolase alpha subunit"
FT                   /id="PRO_0000438117"
SQ   SEQUENCE   101 AA;  11492 MW;  0817758E7CD10567 CRC64;
     MSEKCKKDDW VEIHYVVLEA RERTGDIPED TRKVPLECWI KGWAEKEGTV GEEVTIRTPA
     NRYVKGTLTR INPEYTHTFG PCASELSAIG QELRATLKEG K