ID A0A1J4X6J6_9PROT Unreviewed; 363 AA.
AC A0A1J4X6J6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Erythromycin biosynthesis sensory transduction protein eryC1 {ECO:0000313|EMBL:OIO54055.1};
GN ORFNames=AUJ55_12845 {ECO:0000313|EMBL:OIO54055.1};
OS Proteobacteria bacterium CG1_02_64_396.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1805333 {ECO:0000313|EMBL:OIO54055.1, ECO:0000313|Proteomes:UP000192865};
RN [1] {ECO:0000313|EMBL:OIO54055.1, ECO:0000313|Proteomes:UP000192865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_64_396 {ECO:0000313|EMBL:OIO54055.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO54055.1}.
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DR EMBL; MNWR01000105; OIO54055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4X6J6; -.
DR STRING; 1805333.AUJ55_12845; -.
DR Proteomes; UP000192865; 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 363 AA; 39470 MW; 2B0684D9EC19449F CRC64;
MIPMVDLQGQ YHSIKDEIEQ GMQAVLHSAQ FILGPNVRAF EEEVAAYLGV KHAIGCASGT
DALHLALIAA GVGEGDEVIT TAFTFIATAE AILYVGATPV FVDIDPRTFN LDPNRVEAAI
TPKTKAIIPV HLFGQPADMG ALQGLAAQHH LKIVEDCAQS FGASISGRQT GSLGVAGAFS
FFPSKNLGCY GDGGMVSTDS DEVAAHIRVL RNHGSWQQYH HSELGFNSRL DELQAVVLRV
KLKRIETYNQ GRRRVAQRYS AALAEMGLTP PFEDGLGRHV YHQYTLLTER RDAIMAALRA
GQIGCAVYYP IPLHRQELFT ASGAWQTLPV AESVAARCLS LPIYPELRDD QIDHILETIR
GAL
//
