ID A0A0U5L7J3_9GAMM Unreviewed; 437 AA.
AC A0A0U5L7J3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN Name=alaA {ECO:0000313|EMBL:CUU24742.1};
GN ORFNames=EM595_2511 {ECO:0000313|EMBL:CUU24742.1};
OS Duffyella gerundensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Duffyella.
OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU24742.1, ECO:0000313|Proteomes:UP000059419};
RN [1] {ECO:0000313|Proteomes:UP000059419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Blom J.;
RL Submitted (NOV-2015) 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}.
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DR EMBL; LN907827; CUU24742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5L7J3; -.
DR STRING; 1619313.EM595_2511; -.
DR KEGG; ege:EM595_2511; -.
DR PATRIC; fig|1619313.3.peg.2612; -.
DR Proteomes; UP000059419; Chromosome 1.
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: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:CUU24742.1};
KW Pyruvate {ECO:0000313|EMBL:CUU24742.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW Transferase {ECO:0000313|EMBL:CUU24742.1}.
FT DOMAIN 67..421
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 437 AA; 49282 MW; FCA5C866E90E2EC4 CRC64;
MWSAFSKCRH RSKLSGFGFH GRNDVPPVKA RVMNFQIDKS GKLDGVCYDI RGPVLKEAKR
LEEEGNKVLK LNIGNPAPFG FEAPDEILVD VIRNLPSAQG YCDSKGLYSA RKAIVQHYQA
RDMRDMTVED VYIGNGVSEL IVQSMQALLN MGDEMLVPAP DYPLWTAAVS LSSGKAVHYL
CDEQQGWFPD LDDIRSKITP RTRGIVIINP NNPTGAVYSK ELLMEVVEIA RQHNLIIFAD
EIYDKILYDD AQHHSIAALA PDLLTLTFNG LSKTYRVAGF RQGWMVLNGP KKHAKGYIEG
LEMLASMRLC ANVPAQHAIQ TALGGYQSIS EFIVPGGRLY EQRQRAWEMI NDIPGVSCVK
PQGALYMFPR IDAKKFNLHD DQKMVLDFLL QQKVLLVQGT AFNWPWPDHV RIVTLPRVDE
LEMAIGKFGR FLENYRQ
//
