ID   ORTB_UNKP               Reviewed;         472 AA.
AC   C1FW07;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=2-amino-4-ketopentanoate thiolase beta 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=ortB {ECO:0000303|PubMed:19251850};
GN   ORFNames=DIG-28672_35 {ECO:0000312|EMBL:CAQ42980.1};
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, COFACTOR, SUBSTRATE SPECIFICITY, AND
RP   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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
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 OrtA. {ECO:0000269|PubMed:19251850}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; CU695248; CAQ42980.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1FW07; -.
DR   SMR; C1FW07; -.
DR   KEGG; ag:CAQ42980; -.
DR   BioCyc; MetaCyc:MON-15135; -.
DR   BRENDA; 2.3.1.263; 1522.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; NAS:UniProtKB.
DR   GO; GO:0006591; P:ornithine metabolic process; TAS: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; Transferase.
FT   CHAIN           1..472
FT                   /note="2-amino-4-ketopentanoate thiolase beta subunit"
FT                   /id="PRO_0000438120"
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   472 AA;  51526 MW;  09EC3C611B02BEBB CRC64;
     MAKDTSYDAV MDRRAEIMSR ALGLNYDEFI ISDIAFDYEG MMAKAGYSLE EVRQIQSESG
     VGNTPLLELR NITDLARKTS KRGFGARILI KDEAANPSGS FKDRRASVSI HHAKKLGYPG
     VLAATSGNYG AAVASQAAMK NLGCIIVQEV FDSRHVGQPE IIEKSRKCEA YGAEVVQLTV
     GPELFYVSLI LLEETGYFNA SLYSPFGISG VETLGYELVE QIRARYDKDP AYIVVTHAGG
     GNVTGTARGA LKAGAKNSTI IGASVDLSGL HMASDNDFNK KSFTTGHTGF GVPFATWPDR
     TDVPKNAARP LRYLDRYVTV TQGEVFYVTE ALAQVEGMER GPAGNTSLAA AIALARELPE
     DEIVVVQETE YTGAGKHPWA QLDFAKQNGI AVKRGAPKEN KPGKTIVIPQ NFSQITATEM
     DLNRMRRSYI RNALERNKVK NVTEEDIRFL AEDTKTDADF VTSVIRDLGV RL