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Database: UniProt/TrEMBL
Entry: A0A089YT04_9PSED
LinkDB: A0A089YT04_9PSED
Original site: A0A089YT04_9PSED 
ID   A0A089YT04_9PSED        Unreviewed;       403 AA.
AC   A0A089YT04;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=LT40_05075 {ECO:0000313|EMBL:AIS16820.1};
OS   Pseudomonas rhizosphaerae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS16820.1, ECO:0000313|Proteomes:UP000029499};
RN   [1] {ECO:0000313|EMBL:AIS16820.1, ECO:0000313|Proteomes:UP000029499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS16820.1};
RX   PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA   Kwak Y., Jung B.K., Shin J.H.;
RT   "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT   a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL   J. Biotechnol. 193:137-138(2015).
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; CP009533; AIS16820.1; -; Genomic_DNA.
DR   RefSeq; WP_043193314.1; NZ_CP009533.1.
DR   AlphaFoldDB; A0A089YT04; -.
DR   STRING; 216142.LT40_05075; -.
DR   KEGG; prh:LT40_05075; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000029499; 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:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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:AIS16820.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029499};
KW   Transferase {ECO:0000313|EMBL:AIS16820.1}.
FT   DOMAIN          34..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   403 AA;  44830 MW;  85982AFFB8786A39 CRC64;
     MQFSKSNKLA NVCYDIRGPV LKHAKRLEEE GHRILKLNIG NPAPFGFEAP VEILQDVIRN
     LPTAQGYSDS KGLFSARKAV MQYYQQKQVE GVGIEDIYLG NGVSELIVMS LQALLNNGDE
     VLIPAPDYPL WTASVSLAGG HAVHYLCDEQ ANWWPDLDDI KAKITPNTKA MVIINPNNPT
     GAVYSREVLL GMLELARQHN LVVFSDEIYD KILYDDAVHI CTASLAPDLL CLTFNGLSKS
     YRVAGFRSGW IAISGPKHNA QSYIEGIDIL ANMRLCANVP SQHAIQTALG GYQSINDLVL
     PNGRLLEQRN RTWELLNDIP GVSCVKPMGA LYAFPRIDPK VCPIHNDEKF VLDLLLSEKL
     LVVQGTAFNW PNPDHFRVVT LPRVDDLEQA IGRIGSFLKN YRQ
//
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