ID A0A0S8KVS0_9CHLR Unreviewed; 364 AA.
AC A0A0S8KVS0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Erythromycin biosynthesis sensory transduction protein eryC1 {ECO:0000313|EMBL:KPL25118.1};
GN ORFNames=AMJ93_00840 {ECO:0000313|EMBL:KPL25118.1};
OS Anaerolineae bacterium SM23_84.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL25118.1, ECO:0000313|Proteomes:UP000052016};
RN [1] {ECO:0000313|EMBL:KPL25118.1, ECO:0000313|Proteomes:UP000052016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_84 {ECO:0000313|EMBL:KPL25118.1};
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:KPL25118.1}.
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DR EMBL; LJUZ01000005; KPL25118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KVS0; -.
DR PATRIC; fig|1703388.3.peg.327; -.
DR Proteomes; UP000052016; 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 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 364 AA; 39925 MW; 310140911B03750B CRC64;
MIPFGDLRLQ YQAIKIELDR AIQSVLDEGW YILGVSVSAF ENEFAAYCGT EFAVGVGNGT
DALQLALMAC GIGPGDEVLT TPLSATFTAL AISATGAVPT FLDIDPDTYN MDPQKLEGAI
GPRTKAIMPV HLYGQPADMD PILSLARDHN LLVIEDAAQA HGAVYKGRRA GSLGDVGCFS
FYPSKNLGAF GDGGMVVTDN PAIAERVRML RNGGQKGRYD HQLLGRNSRL DELQAAILRV
KLTYLEKWNE RRRHIAALYT ALLADKVEPP VEMPHVRHVY HLYVIRCKDR DALQKHLGER
GVGTAVHYPT PIHLQGAYRG LNLRPGSFPV AERSAEQVLS LPIYPELTDA KVRQVAAHIL
DWDM
//
