ID A0A0N0TTU9_9PSEU Unreviewed; 369 AA.
AC A0A0N0TTU9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Erythromycin biosynthesis sensory transduction protein eryC1 {ECO:0000313|EMBL:KOX30116.1};
GN ORFNames=ADK67_10285 {ECO:0000313|EMBL:KOX30116.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX30116.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX30116.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX30116.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-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:KOX30116.1}.
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DR EMBL; LGED01000079; KOX30116.1; -; Genomic_DNA.
DR RefSeq; WP_053716162.1; NZ_LGED01000079.1.
DR AlphaFoldDB; A0A0N0TTU9; -.
DR STRING; 1415542.ADK67_10285; -.
DR PATRIC; fig|1415542.3.peg.2227; -.
DR OrthoDB; 5342089at2; -.
DR Proteomes; UP000037722; 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}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 369 AA; 39510 MW; F391C280126E6133 CRC64;
MSDPVAFRDL VAEHATIRDE VVAAVTRVVD AGAFVLGPEL EAFEREWADY CGTSHAVGVG
SGLSAIELIL RAHDVGPGDE VVVPAYTFIA TWLAVSAVGA VPVPVDVDPG AGNIDPAAVE
RAIGPRTVAI IAVHLFGTPA PMTQLRHIAD RRSLLLVEDA AQAHGAEYRG RKCGSLADAA
AFSFYPTKNL GALGDGGVVN TDSATVADRV RSLRNYGSTT RYRHDETATN SRLDEIQAAV
LRVKLRHLDA ANAERRQVAS AYLDLLRADG VRLPVAPPPD EARPSWHIFT LRSDRRDHLR
ARLGQDGIGT QVYYPVPPHR TAAYREFAAL DLPVATDLAR TSLALPCRPG VLPHVPAVAA
SLRNAMEVE
//
