ID A0A0Q9PU03_9ACTN Unreviewed; 404 AA.
AC A0A0Q9PU03;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=ASG76_12235 {ECO:0000313|EMBL:KRE94154.1};
OS Nocardioides sp. Soil774.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736408 {ECO:0000313|EMBL:KRE94154.1, ECO:0000313|Proteomes:UP000051100};
RN [1] {ECO:0000313|EMBL:KRE94154.1, ECO:0000313|Proteomes:UP000051100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE94154.1,
RC ECO:0000313|Proteomes:UP000051100};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE94154.1, ECO:0000313|Proteomes:UP000051100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE94154.1,
RC ECO:0000313|Proteomes:UP000051100};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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}.
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:KRE94154.1}.
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DR EMBL; LMSM01000008; KRE94154.1; -; Genomic_DNA.
DR RefSeq; WP_056603767.1; NZ_LMSM01000008.1.
DR AlphaFoldDB; A0A0Q9PU03; -.
DR STRING; 1736408.ASG76_12235; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000051100; Unassembled WGS sequence.
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:KRE94154.1};
KW Transferase {ECO:0000313|EMBL:KRE94154.1}.
FT DOMAIN 60..396
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 404 AA; 44775 MW; 4652A2F416A59CD7 CRC64;
MRPIRQSKKL QGVRYDVRGP ILVEAQRLEA EGHRILKLNI GNTAPFGFEA PEQIVADMVH
HLPQSQGYAD SQGIWSARTA VMHYYQSHGL RDVGVEDIFI GNGVSELISM VLQAFVDDGN
EILVPSPDYP LWTGAVTLAG GIPVHYRCDE DDDWNPDLAD IEAKITENTH ALVIINPNNP
TGAVYSEEVV KGLVDIARRH QLVVMADEIY EKILFEDAQH HHAATFGGND VLTLTFSGLS
KAYRVCGYRA GWVMISGPKE IATDFLEGLT LIANMRMCAN VPAQHAIQTA LGGYQSVEEL
IGPGGRFYEQ SMLAHRLLNE IPGVSNVKPR GALYCFPRLD PEVYAIDDDQ EFVIDLLRAK
KLLVTHGTGF NWPTPDHFRL VTLPEASVLE EAIGRIADFL ATRR
//
