ID A0A089LSK0_9BACL Unreviewed; 429 AA.
AC A0A089LSK0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Aminotransferase class III {ECO:0000313|EMBL:AIQ62198.1};
GN ORFNames=PSTEL_02775 {ECO:0000313|EMBL:AIQ62198.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ62198.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ62198.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ62198.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP009286; AIQ62198.1; -; Genomic_DNA.
DR RefSeq; WP_038693309.1; NZ_CP009286.1.
DR AlphaFoldDB; A0A089LSK0; -.
DR STRING; 169760.PSTEL_02775; -.
DR KEGG; pste:PSTEL_02775; -.
DR HOGENOM; CLU_016922_10_0_9; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000029507; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AIQ62198.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000029507};
KW Transferase {ECO:0000313|EMBL:AIQ62198.1}.
SQ SEQUENCE 429 AA; 46105 MW; D57F971B1987EDCA CRC64;
MDGQFIGREA VAAKRKQYFY PCTQHFYRDA PQLVRGSMQH VYDENGKKYT DFFAGVSVVA
CGHCNPAITE RTIEQLRRLQ HTTTVYLTEP SVLLAERLES VLPGNLRRTF FVNSGSEANE
GALLLARLHT GRKGFIALES GLHGRTNLTM SVTGLSMWRT DKYLDEDVAF IRRPFDPELT
LAEASEISLA DLKAVLAAKG DTIAALIAEP IQGNGGMIMP EPGYFRAVKE LLELHGILLI
ADEIQTGFGR TGAMFAMEHF GVVPDIVTMA KALGNGVPVA AFAAGDEIAA SLNTPSASTF
GGNPVSAATA LAVLDYIEAE RLPERAALLG ARLKAGLREL QDRYPALVAD VRGTGLMLGM
ELRGAGSAES AALTDDVLED LKNQAYLVGK NGVGRNVLAF QPPLVIMEED IDGLLAALDS
TLARLGAQV
//
