ID   A0A0S8FZV0_9BACT        Unreviewed;       395 AA.
AC   A0A0S8FZV0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=2-amino-3-ketobutyrate CoA ligase {ECO:0000313|EMBL:KPK65498.1};
DE            EC=2.3.1.29 {ECO:0000313|EMBL:KPK65498.1};
GN   ORFNames=AMS21_04540 {ECO:0000313|EMBL:KPK65498.1};
OS   Gemmatimonas sp. SG8_38_2.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703358 {ECO:0000313|EMBL:KPK65498.1, ECO:0000313|Proteomes:UP000051763};
RN   [1] {ECO:0000313|EMBL:KPK65498.1, ECO:0000313|Proteomes:UP000051763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_38_2 {ECO:0000313|EMBL:KPK65498.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPK65498.1}.
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; LJTP01000043; KPK65498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8FZV0; -.
DR   PATRIC; fig|1703358.3.peg.2591; -.
DR   Proteomes; UP000051763; Unassembled WGS sequence.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd06454; KBL_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR13693:SF103; 2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE; 1.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:KPK65498.1};
KW   Ligase {ECO:0000313|EMBL:KPK65498.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:KPK65498.1}.
FT   DOMAIN          43..384
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   395 AA;  42844 MW;  B3E88AF0E8D6D840 CRC64;
     MSGLFERLQS ELHEMREQGV YKQLIHLDSP QDAVVRIDEL GGEVINLCSN NYLGLCNTPE
     VIAAGVAAYK EFGAGTSSVR FICGTFSLHR RLEDKIAAFL GVDSALTYVS CWNANTGLTP
     TFLEEEDALI SDELNHASII DGVRMTRAQR KIYKHSDMDD LEQALKDTAG ARSRFIITDG
     VFSMEGDICR LPDILELAER YDATVAVDDS HATGVLGDTG RGTPEHYGLH GKVPVITSTL
     GKALGGAAGG FTAGPPELTD YLTQRSRPML FSNALPPATT AHSLAAIEHL EKHPELVQKL
     RSNTAYFREK LLEAGFKPIE GDTPIVPIII GETAEAIRMS KMLLEQGVFV IGFGYPVVPH
     GTARIRCQIS AAHDVEHLDA VLDAMKKVGA ELGIT
//