ID A0A0Q4V3I4_9MICO Unreviewed; 403 AA.
AC A0A0Q4V3I4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=ASF23_10890 {ECO:0000313|EMBL:KQO62300.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO62300.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO62300.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62300.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO62300.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62300.1,
RC ECO:0000313|Proteomes:UP000050821};
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 ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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:KQO62300.1}.
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DR EMBL; LMMJ01000009; KQO62300.1; -; Genomic_DNA.
DR RefSeq; WP_055953920.1; NZ_LMMJ01000009.1.
DR AlphaFoldDB; A0A0Q4V3I4; -.
DR STRING; 1736311.ASF23_10890; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000050821; Unassembled WGS sequence.
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; 3.90.1150.10; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; 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:KQO62300.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050821};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KQO62300.1}.
FT DOMAIN 40..398
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 42831 MW; DFB69A10C681B210 CRC64;
MNREAASSAR IARRIAAIAE SATLKVDAKA KALKADGRAI VSFAAGEPDF ATPDHVVEAA
VSAARDPKNH HYTPAVGLPE LRQAIADKTA RVSGATVEPS QVIVTNGGKQ AVYEAFATIV
DEGDEVLLPA PYWTTYPEAI RLAGGSPVEV FAGSDQGYLV TVEQLEAART PRTKALLFCS
PSNPTGAVYS PEQTKAIGEW ALEHGIWVIS DEIYQDLVYD GVVATGILAA VPELADTTIL
VNGVAKTYAM TGWRVGWFIG PADAVAAASN LQSHLSSNVS NVSQRAAIAA LTGPQEPVLA
MREAFDRRRK LIVEGLNAIP GFVTPTPEGA FYVYPDVTAL LGREWKGRQV DTSLELADLI
LEEAEVAAVP GEAFGPSGYL RFSYALGDDD IREGVARLQR LFG
//
