ID   A0A0F2S8U3_9FIRM        Unreviewed;       434 AA.
AC   A0A0F2S8U3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN   ORFNames=VR66_20205 {ECO:0000313|EMBL:KJS47359.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS47359.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS47359.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS47359.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-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   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:KJS47359.1}.
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DR   EMBL; LADV01000243; KJS47359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2S8U3; -.
DR   PATRIC; fig|1629714.3.peg.5771; -.
DR   Proteomes; UP000033503; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; 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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          83..419
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   434 AA;  49199 MW;  C150D1D0B307A6EC CRC64;
     MNEIAQDLNN QIQQENPFVY ELLSELGKNL YYPKGILTQT AEANQKAYRF NATIGIATEN
     GQPMFLPLIQ ETLNNYGPKD LYPYAPPAGK PELRQLWREK MLQENPSLKD KSFSNPIVTN
     ALTHGLSIVA DLFINENDSL VLPDKLWGNY NFIFGVRRGA KNVLFPFYTK DGAFNTAAMR
     EALLSKRDQG KAVLLLNFPN NPTGYTPNEE EAKEIVEALR EVAQQGMNLV VITDDAYYGL
     FYEDSIKESL FARIANIHPR ILAIKVDGAT KEDYMWGFRV GFITYASEHP AVLNALEKKT
     LGIIRGTISS SSHPAQTFVI NALKSSEFLT QKQAKFELLK KRADKVKEVL EHGEYKDAWD
     YYPFNSGYFM CLKLKGVNSE TLRIHLLDHY GVGVISLGED DVRVTFSCVE EQEVKQLFDL
     IYQGFQDLSA KNIK
//