ID A0A0Q8P0K0_9ACTN Unreviewed; 366 AA.
AC A0A0Q8P0K0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Erythromycin biosynthesis sensory transduction protein eryC1 {ECO:0000313|EMBL:KRB67309.1};
GN ORFNames=ASE03_02875 {ECO:0000313|EMBL:KRB67309.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB67309.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB67309.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB67309.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB67309.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB67309.1,
RC ECO:0000313|Proteomes:UP000051829};
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 DegT/DnrJ/EryC1 family.
CC {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:KRB67309.1}.
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; LMHX01000023; KRB67309.1; -; Genomic_DNA.
DR RefSeq; WP_057227379.1; NZ_LMHX01000023.1.
DR AlphaFoldDB; A0A0Q8P0K0; -.
DR STRING; 1736486.ASE03_02875; -.
DR Proteomes; UP000051829; Unassembled WGS sequence.
DR GO; GO:0017000; P:antibiotic biosynthetic process; 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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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 Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000051829}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 366 AA; 38862 MW; D58E892193C14C52 CRC64;
MNPIPLVDLQ AAHAEVAEEV RAGFDRVLTS GAYIKGPDVT AFEAEYAAFS GVSHAVGTAN
GTDAIEMALR ALELPAGARV VLPANTFVAT AEAVVRAGLY PVLVDVDPYA LLIDPARAAE
AAADAYLPVH LNGQLAPMEQ ILELAEGRPV IEDGAQSQGA TRHGRPSGSW GLLAATSFYP
GKNLGAYGDA GAVVTDSAEL AALVREIGDH GSSEKYIHER FGFNSRLDTL QAVVLRAKLR
HLPGWNVARR AAAVRYHQLL AGLPGLTLPV TLPGNEHVWH LYAVRVPRGR DEVLAALHAA
GIGAGIHYPV PVHLQPAFQY LGHPEGSFPV TERAAREILT LPLHPHLTAD QQIFIAETLA
KALARI
//
