ID   K0CHK2_ALCDB            Unreviewed;       391 AA.
AC   K0CHK2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=B5T_03836 {ECO:0000313|EMBL:AFT72098.1};
OS   Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS   B-5) (Alloalcanivorax dieselolei).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alloalcanivorax.
OX   NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT72098.1, ECO:0000313|Proteomes:UP000006286};
RN   [1] {ECO:0000313|EMBL:AFT72098.1, ECO:0000313|Proteomes:UP000006286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC   {ECO:0000313|Proteomes:UP000006286};
RX   PubMed=23144414; DOI=10.1128/JB.01813-12;
RA   Lai Q., Li W., Shao Z.;
RT   "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL   J. Bacteriol. 194:6674-6674(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; CP003466; AFT72098.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0CHK2; -.
DR   STRING; 930169.B5T_03836; -.
DR   KEGG; adi:B5T_03836; -.
DR   PATRIC; fig|930169.3.peg.3790; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_3_6; -.
DR   Proteomes; UP000006286; Chromosome.
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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:AFT72098.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AFT72098.1}.
FT   DOMAIN          35..384
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   391 AA;  42952 MW;  CBBD5F1E511F7B14 CRC64;
     MTDLQRISRL ANTVPPFHVM ALLERAQQLA AQGRDIIHLE VGEPDFPCPS PVMAAARHAL
     DLGQTRYTPA AGLPALREII AEDYRDRFGA QVDPARIVVT PGASGALQLA LGALLDPGDG
     VLLCDPGYPC NRQFVRMFGG IPQPMPLQAS TGFRPSGEIL RCAWDKTTRA AVVASPDNPT
     GNRIPAGELN DWARWCRERQ GTLIVDEIYQ GLCYGAEAET VLAHGDAAWV INSFSKYFGM
     TGWRLGWLVA PEAAVPAVER LAQNWFLAPG TVAQHAAMAA FSEDTLAIAE QRRQLLARRR
     TLLLEALPGM GLPVVGDSEG AFYIYVDVSA HTRDSFELCR RLLEEAGVAV TPGLDFGETH
     QPERYIRLAY TCDEERLHQA LERLARFLER Q
//