ID   KAT_CLOAI               Reviewed;         414 AA.
AC   B0VH76;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=3-aminobutyryl-CoA aminotransferase;
DE            EC=2.6.1.111 {ECO:0000269|PubMed:21826218};
DE   AltName: Full=HemL-like protein;
GN   Name=kat; OrderedLocusNames=CLOAM0809;
OS   Cloacimonas acidaminovorans (strain Evry).
OC   Bacteria; Candidatus Cloacimonetes; Candidatus Cloacimonas.
OX   NCBI_TaxID=459349;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Evry;
RX   PubMed=18245282; DOI=10.1128/jb.01248-07;
RA   Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA   Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA   Weissenbach J., Le Paslier D.;
RT   "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT   provides a first glimpse of a new bacterial division.";
RL   J. Bacteriol. 190:2572-2579(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=Evry;
RX   PubMed=21826218; DOI=10.1371/journal.pone.0022918;
RA   Perret A., Lechaplais C., Tricot S., Perchat N., Vergne C., Pelle C.,
RA   Bastard K., Kreimeyer A., Vallenet D., Zaparucha A., Weissenbach J.,
RA   Salanoubat M.;
RT   "A novel acyl-CoA beta-transaminase characterized from a metagenome.";
RL   PLoS ONE 6:E22918-E22918(2011).
CC   -!- FUNCTION: 3-aminobutyryl-CoA aminotransferase that acts specifically on
CC       coenzyme A (CoA) esters and catalyzes the conversion of 3-aminobutyryl-
CC       CoA into acetoacetyl-CoA in an alternative pathway of lysine
CC       fermentation. {ECO:0000269|PubMed:21826218}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-aminobutanoyl-CoA + 2-oxoglutarate = acetoacetyl-CoA +
CC         L-glutamate; Xref=Rhea:RHEA:50936, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57286, ChEBI:CHEBI:57366;
CC         EC=2.6.1.111; Evidence={ECO:0000269|PubMed:21826218};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:21826218};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.3 uM for 3-aminobutyryl-CoA {ECO:0000269|PubMed:21826218};
CC         KM=2.9 uM for alpha-ketoglutarate {ECO:0000269|PubMed:21826218};
CC         KM=20.1 uM for pyruvate {ECO:0000269|PubMed:21826218};
CC         Note=kcat is 1.80 sec(-1) for 3-aminobutyryl-CoA. kcat is 1.80 sec(-
CC         1) for alpha-ketoglutarate. kcat is 0.4 sec(-1) for pyruvate.;
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:21826218};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC       pathway.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21826218}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; CU466930; CAO80691.1; -; Genomic_DNA.
DR   RefSeq; WP_015424550.1; NC_020449.1.
DR   AlphaFoldDB; B0VH76; -.
DR   SMR; B0VH76; -.
DR   STRING; 459349.CLOAM0809; -.
DR   EnsemblBacteria; CAO80691; CAO80691; CLOAM0809.
DR   KEGG; caci:CLOAM0809; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_4_0; -.
DR   OMA; GYNGWHD; -.
DR   OrthoDB; 493793at2; -.
DR   BRENDA; 2.6.1.111; 14207.
DR   UniPathway; UPA00870; -.
DR   Proteomes; UP000002019; Chromosome.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR   GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR   GO; GO:0019475; P:L-lysine catabolic process to acetate; IDA:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..414
FT                   /note="3-aminobutyryl-CoA aminotransferase"
FT                   /id="PRO_0000424019"
FT   MOD_RES         261
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   414 AA;  46481 MW;  2FFC3433D7BD095A CRC64;
     MAEKLKLARS MSLFEEAKQL VPGGVAGIRR PYNFVPGEYP IFFDHGKGGR VVDVDGNEYI
     DFLCAYGPII IGYREDEIDD AVINQIKNKG FCFSLTQEMQ NTLVKKLREL IPCCEMAALV
     KTGSDATTIA IRVARGYTGK TKIARYGYHG WHDWCVEVKG GIPPKLYEDI YEFHYNDLDS
     LKAILEANKD DMAGIIITPI GHPNGAEVQM PKPGYLEAVR ELANQYHCLL IFDEIRSGFR
     CSLGGAQKLF GVTPDLSTFG KAMANGYAIA ALVGKEEYMQ VLADKVFLSS TFFPNSDGIV
     AAIKTIEILE RDRILDVVAA KGRKFGAEVE KVVEESGVPV NFTGAPWMPY ITFKKDEAGL
     YKKLRTEYYT QLIRHNVFMQ PYHHGYICYR HTDEDLAYTV EAIRESLAEV KKML