ID A0A2M9EBG9_9GAMM Unreviewed; 364 AA.
AC A0A2M9EBG9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Erythromycin biosynthesis sensory transduction protein eryC1 {ECO:0000313|EMBL:PJK01615.1};
GN ORFNames=CO611_00555 {ECO:0000313|EMBL:PJK01615.1};
OS Xanthomonadaceae bacterium NML03-0222.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032581 {ECO:0000313|EMBL:PJK01615.1, ECO:0000313|Proteomes:UP000229850};
RN [1] {ECO:0000313|EMBL:PJK01615.1, ECO:0000313|Proteomes:UP000229850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML03-0222 {ECO:0000313|EMBL:PJK01615.1,
RC ECO:0000313|Proteomes:UP000229850};
RA Bernier A.-M., Bernard K.;
RT "Zoonotically transmitted species of Xanthomonadaceae : Genome sequencing
RT and assembly.";
RL Submitted (SEP-2017) 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:PJK01615.1}.
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DR EMBL; NWQM01000001; PJK01615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9EBG9; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000229850; 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:UP000229850}.
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 187
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 364 AA; 39470 MW; 6DF8B048583D426A CRC64;
MPLPINDLKR HIAPLKDLLS SCSTAVIESG HYVLGPGVTQ FETEFAAYCG VKHCIGVANG
TDALELALKS VSVEPGTAVG VVANAAMYGT SAVLACSASP VFIDVEENSA NMSLEHLTEV
LQKNSLKAII ITHLYGRLAN VKSIIALCKA QGVAVVEDCA QAHGARLEGK AAGSFGDAAA
FSFYPTKNLG ALGDGGAVVT NNEEAAQRAR QLRQYGWTAK YTNTFRGGRN SRLDEIQAKM
LSKMLPLLDG WNARRREIAN IYSSKINNPK IQTPPISGEE YVGHLYVIHS QEREALKEHL
LKYEILTDIH YPIPDHHQPC HAGAYDDLRL PVTEKLAKTA LTLPCFPELT DEEAMQVVEA
CNQF
//
