ID A0A0E3ZKL9_9BURK Unreviewed; 422 AA.
AC A0A0E3ZKL9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=CL55_00014880 {ECO:0000313|EMBL:AKD25821.1};
OS Polynucleobacter duraquae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1835254 {ECO:0000313|EMBL:AKD25821.1, ECO:0000313|Proteomes:UP000061135};
RN [1] {ECO:0000313|EMBL:AKD25821.1, ECO:0000313|Proteomes:UP000061135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-MoK4 {ECO:0000313|EMBL:AKD25821.1,
RC ECO:0000313|Proteomes:UP000061135};
RA Hahn M.W.;
RT "Genome of Polynucleobacter strain MWH-MoK4.";
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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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; CP007501; AKD25821.1; -; Genomic_DNA.
DR RefSeq; WP_046330530.1; NZ_CP007501.1.
DR AlphaFoldDB; A0A0E3ZKL9; -.
DR STRING; 1835254.CL55_00014880; -.
DR KEGG; pdq:CL55_00014880; -.
DR PATRIC; fig|576611.7.peg.1514; -.
DR HOGENOM; CLU_017584_4_2_4; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000061135; Chromosome.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009042; F:valine-pyruvate transaminase activity; IEA:UniProtKB-EC.
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; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 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:AKD25821.1};
KW Transferase {ECO:0000313|EMBL:AKD25821.1}.
FT DOMAIN 34..394
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 422 AA; 46976 MW; 3729EAC246961A2B CRC64;
MKPILKSAKL NHVCYDIRGP VLELAQRMEE EGHKIIKLNI GNVGVFGFDP PEEIQLDMIR
NLGNASAYSD SKGIFAARKA IMQYCQEKGI QGVTLDDIYT GNGVSELIVL AMNALLNNGD
EVLVPAPDYP LWTAAVSLSG GTPVHYLCDE SKEWAPDLAD LRKKITARTK AIVVINPNNP
TGAIYSKEVL TELCSIAREH DLILFADEIY DKMLYDKEKH VSLASLSTDV VTITFNGLSK
NYRSCGYRAG WMVVSGDKEM IRDYIEGLNM LSSMRLCANV PGQYAIQTAL GGYQSINDLV
AEGGRLAKQR DLAWKLITEI PGVTCVKPKS ALYLFPKLDA EMYPIEDDQQ FVADFLKEEK
VLLVQGSGFN WIKSDHFRVV FLPHEDVLKE AIGRLARFLE RYRQKHSRKA TSSTNSTATK
AS
//