ID   C6J1T5_9BACL            Unreviewed;       433 AA.
AC   C6J1T5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Aminotransferase, class I/II {ECO:0000313|EMBL:EES72955.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:EES72955.1};
GN   ORFNames=POTG_02362 {ECO:0000313|EMBL:EES72955.1};
OS   Paenibacillus sp. oral taxon 786 str. D14.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=621372 {ECO:0000313|EMBL:EES72955.1, ECO:0000313|Proteomes:UP000003981};
RN   [1] {ECO:0000313|EMBL:EES72955.1, ECO:0000313|Proteomes:UP000003981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D14 {ECO:0000313|EMBL:EES72955.1,
RC   ECO:0000313|Proteomes:UP000003981};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., White A.,
RA   Lander E., Nusbaum C., Galagan J., Birren B.;
RT   "The Genome Sequence of Paenibacillus sp. D14.";
RL   Submitted (MAR-2009) 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}.
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DR   EMBL; GG695977; EES72955.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6J1T5; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_052346_1_0_9; -.
DR   Proteomes; UP000003981; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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;
KW   Aminotransferase {ECO:0000313|EMBL:EES72955.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003981};
KW   Transferase {ECO:0000313|EMBL:EES72955.1}.
FT   DOMAIN          70..421
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   433 AA;  47869 MW;  0645174F4D4CBEBA CRC64;
     MMNPLAEQLN ESVKSGNRHV YDMLSTLGKE IYFPKEGILS QSAEASAHAK KYNATIGIAT
     ENGIPMHLAA IQDTLSAYKP QDLYPYAPPA GKPELRSVWR DKMIQENPSL EGKSFGQPIV
     TNALTHGLSI VADLFVDEGD VVIYPDKNWE NYELTFGIRR HADIVNFPLF TEDMTFNSAG
     LREALLAQKD KGKAIVILNF PNNPTGYTPG AKEGGEIVAA IQAAAEEGIN VVVVTDDAYF
     GLFFEDSLHE SLFGKLAGLH PRILPIKVDG ATKEEYVWGF RVGFITYAAE DQAVLTALEQ
     KTLGIIRATI SSGAHPSQTF VLHALKSPEF TAQKEEKFRI MKGRANKVKA LLDSGKYGDV
     WEYYPFNSGY FMCLKLKTVA AEALRQHLIH QYGIGTIALG DTDLRIAFSC IAEEHLEELF
     DLIYQGVQDL QGK
//