ID   A0A257KMP5_9BRAD        Unreviewed;       446 AA.
AC   A0A257KMP5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OYU88653.1};
GN   ORFNames=CFE29_20445 {ECO:0000313|EMBL:OYU88653.1};
OS   Bradyrhizobiaceae bacterium PARB1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=2015576 {ECO:0000313|EMBL:OYU88653.1, ECO:0000313|Proteomes:UP000216768};
RN   [1] {ECO:0000313|EMBL:OYU88653.1, ECO:0000313|Proteomes:UP000216768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PARB1 {ECO:0000313|EMBL:OYU88653.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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}.
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:OYU88653.1}.
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; NKIY01000005; OYU88653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257KMP5; -.
DR   Proteomes; UP000216768; Unassembled WGS sequence.
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:OYU88653.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:OYU88653.1}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  48181 MW;  527967B8B1896AEC CRC64;
     MSVTPAQRGK MVNGFDPATA ESLTPESRKL VERRIALLGP AYRLFYKDPV EVARANGVLL
     YDSEGNEYLD AYNNVVSIGH CHPRVVEAIT KQAQTICSHT RYIQKGILDY AEQLLATFDG
     PARHAMFTCT GSEANDLAVR MAKHHTGNQG IIITDEAYHG NSELTAGFSP SLGPFSPLGA
     FVRRVPAPDS YRIAPENMGK WMAEKVSEQI VDLQRRGAGV ACFIADSMFS SDGIFSHPTN
     LLQPVVDVVH KAGGIYIADE VQSGFGRSGE KLWGYQRHGI TPDIITMGKP MGNGYPVAAA
     VMLPEIVEKF GRDNRYFNTF GGNTVAMAAA QAVLNVIQDE KLVENSLKVG KLLREGFEAL
     AKKYQGIGDV RGSGLYVGVE MVKNRTTKEP DAAAAAAIVN GLRARRVLIS ATGAAANTLK
     IRPPLVFTAA HADRLLTEAD AVFATL
//