ID   A0A0M0BID7_9ARCH        Unreviewed;       402 AA.
AC   A0A0M0BID7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=2-amino-3-ketobutyrate CoA ligase {ECO:0000313|EMBL:KON28313.1};
GN   ORFNames=AC480_04095 {ECO:0000313|EMBL:KON28313.1};
OS   miscellaneous Crenarchaeota group archaeon SMTZ1-55.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1685133 {ECO:0000313|EMBL:KON28313.1, ECO:0000313|Proteomes:UP000037456};
RN   [1] {ECO:0000313|EMBL:KON28313.1, ECO:0000313|Proteomes:UP000037456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ1-55 {ECO:0000313|EMBL:KON28313.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KON28313.1}.
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DR   EMBL; LFWX01000065; KON28313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BID7; -.
DR   PATRIC; fig|1685133.3.peg.489; -.
DR   Proteomes; UP000037456; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; 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; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   PANTHER; PTHR13693:SF3; LD36009P; 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   Ligase {ECO:0000313|EMBL:KON28313.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693}.
FT   DOMAIN          46..391
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   402 AA;  44140 MW;  142820FCE7001F79 CRC64;
     MNVTGTRHPT KYLGDEYRRL VRESLNWELK VLESASEPVC RVNGQEVIML CANNYLNLAT
     HPKVVNAAIE ATRKYGAGAG SDRSISGNML VHEELDKRLA RFKKAPASLT FQTGYMTNQG
     VIPQLADRGD LFVSDELNHG SIIDGVRLSH ADRAVFKHKD VEDLARVMDA AETHDPPYRH
     IWILTDGVFS MDGDLAPLRA IADIAKEHHA GVYVDDAHGE GVLGTAGRGI VDHFHLGRDE
     VHVEMGTFSK AFGVVGGHIT GSEDLRNFAY NTVRTWLLSA AVPPGVAAAC IAAIDVLETE
     PEHVTKVWAN RNHLLDSLQD AGFDTGHSET PIIPVMCGRS KKARDLANYL WTQGIFVLPI
     FFPMVARGQA RIRVQLCTKH TPDQLEKTVA AFETGGRKLG LI
//