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Database: UniProt
Entry: F1YUJ1_9PROT
LinkDB: F1YUJ1_9PROT
Original site: F1YUJ1_9PROT 
ID   F1YUJ1_9PROT            Unreviewed;       378 AA.
AC   F1YUJ1;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Pleiotropic regulatory protein {ECO:0000313|EMBL:EGE47630.1};
GN   Name=degT {ECO:0000313|EMBL:EGE47630.1};
GN   ORFNames=APO_1613 {ECO:0000313|EMBL:EGE47630.1};
OS   Acetobacter pomorum DM001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=945681 {ECO:0000313|EMBL:EGE47630.1, ECO:0000313|Proteomes:UP000018454};
RN   [1] {ECO:0000313|EMBL:EGE47630.1, ECO:0000313|Proteomes:UP000018454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DM001 {ECO:0000313|EMBL:EGE47630.1,
RC   ECO:0000313|Proteomes:UP000018454};
RX   PubMed=22053049; DOI=10.1126/science.1212782;
RA   Shin S.C., Kim S.H., You H., Kim B., Kim A.C., Lee K.A., Yoon J.H.,
RA   Ryu J.H., Lee W.J.;
RT   "Drosophila microbiome modulates host developmental and metabolic
RT   homeostasis via insulin signaling.";
RL   Science 334:670-674(2011).
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:EGE47630.1}.
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DR   EMBL; AEUP01000028; EGE47630.1; -; Genomic_DNA.
DR   RefSeq; WP_006116689.1; NZ_AEUP01000028.1.
DR   AlphaFoldDB; F1YUJ1; -.
DR   OrthoDB; 9768668at2; -.
DR   Proteomes; UP000018454; 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:UP000018454}.
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   378 AA;  41598 MW;  05C896DEB2B974EE CRC64;
     MNSSQNRPIA FLDLAAQQKR LEPALRQRLE AVLAHCRFVM GPEVLELEQR LAQWCGAQEC
     VGVSSGTDAL QIVMMGEQIG RDDAVFLPAF TYTATAEVPL VLGATPVFVD VDPQTFQIDP
     EHLRKRIRAV REVGKLKPRA IVGVDLFGQP APWAELRAIA QEEDLFLLAD CAQSFGAKLN
     GTPLGREATA TTLSFFPSKP LGGYGDGGAI LTDDPERAAL YRSLRTHGEG TTRYEVLRTG
     MNGRLDTLQA AVLLAKLDDF TRELTRREEI ACQYDAGLKD VVQVPARVPD SQSAWAIYSV
     LLKNSAEREQ MQARLKEQGV PSAIYYPLPL HKQPAYRDHH DGTALPVSED LAQRILALPI
     HPELTDEEVA RVIAAVRG
//
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