ID A0A0F0HJP0_9PSEU Unreviewed; 368 AA.
AC A0A0F0HJP0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Erythromycin biosynthesis sensory transduction protein eryC1 {ECO:0000313|EMBL:KJK55824.1};
GN ORFNames=UK12_26215 {ECO:0000313|EMBL:KJK55824.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK55824.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK55824.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK55824.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJK55824.1}.
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DR EMBL; JYJF01000104; KJK55824.1; -; Genomic_DNA.
DR RefSeq; WP_045305628.1; NZ_JYJF01000104.1.
DR AlphaFoldDB; A0A0F0HJP0; -.
DR PATRIC; fig|1427391.3.peg.716; -.
DR OrthoDB; 5342089at2; -.
DR Proteomes; UP000033409; 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: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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000033409}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 368 AA; 39011 MW; 5DFDD3F8C997FC40 CRC64;
MTAIPLVDLQ AAHAEVAEEV REGFDRVLAT GAYIKGPDVA AFEAEYAEFS GVRHAVGTAN
GTDALELALR ALRLAPGAGV VLPANTFVAT AEAVVRAGLR PVLVDVDPEH LLIDPAQAAE
ALPGSAALIP VHLNGQLAPM QPLLDLADGR PVIEDGAQSQ GARQHGRVSG SWGRISATSF
YPGKNLGAYG DAGAVVTDDE ELAAAVRLIG DHGSGRKYVH ETFGFNSRLD TLQAVVLRAK
LRRLPGWNEA RRAAAARYDE LLGGLDGISL PRTLPGNEHV WHLYAVRVER GRDEVLAELQ
ANGIGAGIHY PVPVHLQPAF RGLGYAEGSF PVTERAAGEI LTLPLFPQIT EDQQMRVAEA
LAKALTRS
//
