ID A0A150AGT1_9BACT Unreviewed; 394 AA.
AC A0A150AGT1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glutamine--scyllo-inositol aminotransferase {ECO:0000313|EMBL:KXX69139.1};
GN ORFNames=AVL50_17015 {ECO:0000313|EMBL:KXX69139.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX69139.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX69139.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX69139.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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:KXX69139.1}.
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DR EMBL; LQAQ01000089; KXX69139.1; -; Genomic_DNA.
DR RefSeq; WP_062618040.1; NZ_LQAQ01000089.1.
DR AlphaFoldDB; A0A150AGT1; -.
DR STRING; 1775430.AVL50_17015; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000075267; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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 Aminotransferase {ECO:0000313|EMBL:KXX69139.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000075267};
KW Transferase {ECO:0000313|EMBL:KXX69139.1}.
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 394 AA; 43752 MW; D5DEA0FFC029D01C CRC64;
MPGTEYFGAE ERKEVNDVLE SGMLFRYNHD DQRNGHWKAR EFEQLFEEYT GANHAHAVSS
GSAAVACMMA AAGIGHGDEV ICTPFTFIAP IEAVLFAGGI PVFAEVDETL NLSAASIEAA
ITPRTKAVLL VHMCGAAADL DGIKAVCDKH NIKLLEDAGQ ALGAFYKGKH VGLFGEAGAV
SFDFFKITTA GEGGVCFTND KDKYEVMAQF SDHGHSHVGD NRGMEAHPVL GFNYRLGELN
AAIAVAQMRK LEMIRANNKK NKAILKDRLK NEVPFITFRC LPDEEGDSAT FLNFFMETPE
LAEKASKEVQ GVAYWYTNMY HFINQWDHLK ALKSPYKLAI HDYEHRQDWN NIELPKSQNI
IGRLLSIGIR ATWTEEEINA FADQLIAQLK KVVE
//
