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Database: UniProt
Entry: A0A158M297_9BORD
LinkDB: A0A158M297_9BORD
Original site: A0A158M297_9BORD 
ID   A0A158M297_9BORD        Unreviewed;       384 AA.
AC   A0A158M297;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:KAK88057.1};
GN   ORFNames=L497_0830 {ECO:0000313|EMBL:KAK88057.1};
OS   Bordetella holmesii CDC-H585-BH.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK88057.1, ECO:0000313|Proteomes:UP000026682};
RN   [1] {ECO:0000313|EMBL:KAK88057.1, ECO:0000313|Proteomes:UP000026682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK88057.1,
RC   ECO:0000313|Proteomes:UP000026682};
RA   Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P.,
RA   Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J.,
RA   Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L.M., Sanka R., Kim M.,
RA   Losada L.;
RT   "Genome sequence of Bordetella holmseii.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KAK88057.1}.
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DR   EMBL; JFZZ01000125; KAK88057.1; -; Genomic_DNA.
DR   RefSeq; WP_005013387.1; NZ_JFZZ01000125.1.
DR   AlphaFoldDB; A0A158M297; -.
DR   STRING; 35814.BBB42_07445; -.
DR   GeneID; 56625275; -.
DR   PATRIC; fig|1331206.3.peg.3057; -.
DR   Proteomes; UP000026682; 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; 3.40.640.10; 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   PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:KAK88057.1};
KW   Transferase {ECO:0000313|EMBL:KAK88057.1}.
FT   DOMAIN          32..379
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   384 AA;  41469 MW;  47CDC0452A698D54 CRC64;
     MPRLARRTND FLTFQVVELF KEAQALSAAG RDIISLGIGE PDFTAPPQVI EALERASRAG
     LSGYCAPGGL MPLREAIAQF YADEFGAPIH PERVIVTAGA SGALALASAA LVNPGAEVLM
     PDPSYPANSN FVLAAGGVPR LVPSNAAKRF QLSAADVREN WTTATEGVLI ASPSNPTGTS
     IASDELAALL AEVRQRGGYT IMDEIYLGLT YGQTPRSALT LDDDIIVINS FSKYFHMTGW
     RLGWMIVPQA MVSTIEKMSA SLQICAPTLA QHAALACFKP DALKIYAQRR DAFRQRRDYL
     LPEFERLGIP VPVKPDGAFY IYADIRHLGM DSMAFSQRLL HEAGVAAVPG VDFGPAHGLS
     TMRFSYATGL DRLQEAIGRI ERLL
//
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