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Database: UniProt
Entry: A0A0S8J797_9BACT
LinkDB: A0A0S8J797_9BACT
Original site: A0A0S8J797_9BACT 
ID   A0A0S8J797_9BACT        Unreviewed;       379 AA.
AC   A0A0S8J797;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-NOV-2023, entry version 23.
DE   RecName: Full=Erythromycin biosynthesis sensory transduction protein eryC1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMJ85_11445 {ECO:0000313|EMBL:KPL05647.1};
OS   candidate division BRC1 bacterium SM23_51.
OC   Bacteria; Candidatus Sumerlaeota.
OX   NCBI_TaxID=1703761 {ECO:0000313|EMBL:KPL05647.1, ECO:0000313|Proteomes:UP000051549};
RN   [1] {ECO:0000313|EMBL:KPL05647.1, ECO:0000313|Proteomes:UP000051549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_51 {ECO:0000313|EMBL:KPL05647.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPL05647.1}.
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DR   EMBL; LJUL01000284; KPL05647.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8J797; -.
DR   Proteomes; UP000051549; 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        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         186
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   379 AA;  42210 MW;  1F144841A2572276 CRC64;
     MQVPFVNLKA QYDEVRAEID AAWQEAVSRS AFIGGEAVRK FEILLAERFR VKHACGVASC
     TAALTAVLRS LELSPGDEVI TTVHTAAPTA EAIVLAGANV VFCDVEEDTF QIDPAAVETA
     ITPRTRAIVL VHLYGLAARV REIQAVARKH DLVVIEDIAQ AQGARYDARP VGTFGAAGCL
     SFFPSKNLGA FGDGGAVVTN NEEIARFVRM YSNHGRLEKF EHRILGANER LDALQAAILR
     VKLRRLEPWN ERRRQAATWY EQRLADVKEV RLPRPIPQCT PAWHLYVIRI DGRDELAHFL
     KDRGVSTGLH YPLPLHLQPA FSFLGKGEGD FPVAERLARH EILSLPMFPH IEEGQVDCVC
     RTIRQFVAQN LKRTRSTIP
//
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