ID A0A1U7MRD1_9MICO Unreviewed; 374 AA.
AC A0A1U7MRD1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Pyridoxal-5'-phosphate-dependent protein {ECO:0000313|EMBL:OLT21790.1};
GN ORFNames=BJF81_14665 {ECO:0000313|EMBL:OLT21790.1};
OS Ornithinimicrobium sp. CNJ-824.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT21790.1, ECO:0000313|Proteomes:UP000185694};
RN [1] {ECO:0000313|EMBL:OLT21790.1, ECO:0000313|Proteomes:UP000185694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT21790.1,
RC ECO:0000313|Proteomes:UP000185694};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT21790.1}.
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DR EMBL; MKKA01000018; OLT21790.1; -; Genomic_DNA.
DR RefSeq; WP_075957958.1; NZ_MKKA01000018.1.
DR AlphaFoldDB; A0A1U7MRD1; -.
DR STRING; 1904966.BJF81_14665; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000185694; Unassembled WGS sequence.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000185694}.
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 374 AA; 40798 MW; 2A6EA52654F3E0EE CRC64;
MSDRIFLSQA HVTELEEEYV LRALRSGWVA PLGPDVDAFE DEIAERVGVK HALALSSGTA
ALHLALLHLG ARPGTVVVVP SMTFAASANA IAYTGADPVF VDSQTSDGNV DPALLIEAVD
VLRSEGREVV AAMTVDLFGR TCDYERMVPA LAERGVPLLE DAAEALGASS HGNQAGSFGL
AATLSFNGNK IMTTSGGGML LSDDTRLVDH CRKLSTQSRE PVAWYEHAEI GYNYRLSNLL
AALGRAQLTR LDEMIQRRQE IYDQYVTLLS DLPLRFLQSA DHSKIDNHWL TTVVFEDDTV
DVDTIVRDLG LEGIEVRHLW KPMHLQPVFG TSRFFGGAVS EGLFKNGLAL PSGFRLRDQD
INRVAARLRE AVIA
//
