ID A0A0Q7KH70_9ACTN Unreviewed; 453 AA.
AC A0A0Q7KH70;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASD10_00175 {ECO:0000313|EMBL:KQX73735.1};
OS Aeromicrobium sp. Root472D3.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736540 {ECO:0000313|EMBL:KQX73735.1, ECO:0000313|Proteomes:UP000050971};
RN [1] {ECO:0000313|EMBL:KQX73735.1, ECO:0000313|Proteomes:UP000050971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root472D3 {ECO:0000313|EMBL:KQX73735.1,
RC ECO:0000313|Proteomes:UP000050971};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX73735.1, ECO:0000313|Proteomes:UP000050971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root472D3 {ECO:0000313|EMBL:KQX73735.1,
RC ECO:0000313|Proteomes:UP000050971};
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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:KQX73735.1}.
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DR EMBL; LMET01000001; KQX73735.1; -; Genomic_DNA.
DR RefSeq; WP_056602915.1; NZ_LMET01000001.1.
DR AlphaFoldDB; A0A0Q7KH70; -.
DR STRING; 1736540.ASD10_00175; -.
DR OrthoDB; 4510254at2; -.
DR Proteomes; UP000050971; 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:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF3; GAMMA-AMINOBUTYRATE TRANSAMINASE POP2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000050971};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 453 AA; 48610 MW; 2906CE5FF8CE7964 CRC64;
MSIADLDRDY VFHPFTVLAT HQQSGPPISI VEAHGSTVVD ADGRRYLDAM AGLWCVNIGY
SHPEMADALH RQASKLPYFH AFSSMGTEAP ARLAERLIQM APVPMAKVFF GNSGSDANDT
QAKLVWYYNN LLGRPEKKKI ISRHRGYHGV TVLSGGLTGL ANLHDGFDLP LPMIRHVRPP
HRLWEREPGA TDEEFARTLA QELDDLIVAE GPDTVAAFIA EPVMAAGGVI VPPETYFPEI
QKVLDTHDVL LIADEVVCGF GRLGVEFGST AVGARPDLMT VAKGITSAYV PLSACLVGSK
VWDVIVEGSS RYGAFGHGYT YSAHPLAAAA AMTNLDIIER DGLVQRAGDL GTLLHSELRS
AFADHPNVAE IRGTGLVAAV EFVKDPASRT PFDAVGQFSA AVTRASLENG VVTRALPAAD
TVSFSPPFTT TEDEIRAMVD GVRRAAESVA VKA
//
