ID A0A0Q5CLK9_9MICO Unreviewed; 379 AA.
AC A0A0Q5CLK9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:KQQ27652.1};
GN ORFNames=ASF54_02385 {ECO:0000313|EMBL:KQQ27652.1};
OS Frondihabitans sp. Leaf304.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ27652.1, ECO:0000313|Proteomes:UP000051456};
RN [1] {ECO:0000313|EMBL:KQQ27652.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27652.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ27652.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27652.1,
RC ECO:0000313|Proteomes:UP000051456};
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:KQQ27652.1}.
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DR EMBL; LMNV01000002; KQQ27652.1; -; Genomic_DNA.
DR RefSeq; WP_055958368.1; NZ_LMNV01000002.1.
DR AlphaFoldDB; A0A0Q5CLK9; -.
DR STRING; 1736329.ASF54_02385; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000051456; 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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KQQ27652.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051456};
KW Transferase {ECO:0000313|EMBL:KQQ27652.1}.
FT DOMAIN 28..373
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 379 AA; 41310 MW; 8B733AED288718CE CRC64;
MPSLAPHIES VPGSGIRRVF EIAMKLDDVT MLVVGEPDVP VARHIIDAAR RAWAEDRTGY
TPNGGITPLR EALVAKLARE NQIQADVEQV WVTVGATQAL HQAMGLVLSP GSEILVPDPG
YTTFTMNAHM LDARAVPYQL APEAEFQPDL EALEHLVTDR TRAIIVNSPS NPLGVVFGEA
TLRRILDFAK RHDLWVISDE VYEYFTYGPK HVSLAALDDD DRVFSVFSLS KTYAMTGVRV
GYLVTPKGLA DTMRTVQEAQ ISCVAEPDQY AALAAVTGDN QPVADAREHY RENLDLARGL
LDERGIAYLD PEGAFYLWID VSHASRGDVA TWAEDFLLSH RVAVAPGSAF GRTGEGWIRI
SLASPADALT RGLSALPAP
//
