ID I0L0H3_9ACTN Unreviewed; 400 AA.
AC I0L0H3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Putative pyridoxal phosphate-dependent aminotransferase epsN {ECO:0000313|EMBL:CCH17320.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:CCH17320.1};
GN ORFNames=MILUP08_42241 {ECO:0000313|EMBL:CCH17320.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH17320.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:CCH17320.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAIE01000017; CCH17320.1; -; Genomic_DNA.
DR AlphaFoldDB; I0L0H3; -.
DR STRING; 1150864.MILUP08_42241; -.
DR eggNOG; COG0399; Bacteria.
DR Proteomes; UP000003448; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CCH17320.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448};
KW Transferase {ECO:0000313|EMBL:CCH17320.1}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 400 AA; 42347 MW; 3BC1815EEEB96DA4 CRC64;
MPVPGRLADV ADSPPRPHTG DTVYLSPPDV GPLEESYLIA ALRSGWVAPV GPDLQAFEHD
VATRVGTGGA VAVNSGTAAL HLALLGVGVG PTDVVIVPTL TFVATANAAR YIGARPVFVD
CDPRTGNVDV DLAADLIRAL RARGERVGAI VPVDMFGSCA DYGALLPLCA ETDVPVVEDA
AEALGACHAG RPAGSFGRVG VLSFNGNKIM TTSGGGMLVC DDAALLARAR HLATQAREPA
RHYEHHETGY NYRLSNLLAA LGRAQLLRLD QMIARRRHLR DEYAKLFAPV PGVRLVGAQD
AESNCWLTVI AVEPQRCGWR ADDLARHLAE RNIETRPVWK PMHLQPMHAG AESLLTGAAE
RLFTDGLTLP SGSALTEPQI ARVLAAIDEF LSARTGPSLS
//
