ID G9ETV2_9GAMM Unreviewed; 379 AA.
AC G9ETV2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:EHL29303.1};
GN ORFNames=LDG_8738 {ECO:0000313|EMBL:EHL29303.1};
OS Legionella drancourtii LLAP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=658187 {ECO:0000313|EMBL:EHL29303.1, ECO:0000313|Proteomes:UP000002770};
RN [1] {ECO:0000313|EMBL:EHL29303.1, ECO:0000313|Proteomes:UP000002770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LLAP12 {ECO:0000313|EMBL:EHL29303.1,
RC ECO:0000313|Proteomes:UP000002770};
RX PubMed=22047552; DOI=10.1186/1471-2164-12-542;
RA Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D., Fournier P.E.,
RA Greub G.;
RT "Insight into cross-talk between intra-amoebal pathogens.";
RL BMC Genomics 12:542-542(2011).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; JH413848; EHL29303.1; -; Genomic_DNA.
DR RefSeq; WP_006872606.1; NZ_JH413848.1.
DR AlphaFoldDB; G9ETV2; -.
DR STRING; 658187.LDG_8738; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_0_6; -.
DR InParanoid; G9ETV2; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000002770; 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:SF9; PROTEIN RV3402C; 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:EHL29303.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002770};
KW Transferase {ECO:0000313|EMBL:EHL29303.1}.
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 379 AA; 43396 MW; E120136F03C8C0B4 CRC64;
MAIQVFVPKF RTEECLEEIR ECLDKSWTGL GFKTQIFEEK WNDYTGLPHS HFINSNTVGL
HLAFNLFKSH YGWQNDDEVI TTPLTFISTN HAIVYEKLKP VFADVDSTSC LSPESIEAHI
TAKTRAVIYV GIGGNTGRLE DVANLCKKHN LKLILDAAHM AGTRYKGKHI GHEADVTIFS
FQAVKNLPTA DSGMICFKDK FFDEECRKLT WLGINKDTFA RTTKQGNYKW KYDVESIGFK
YHGNSIMASL GIVALKYLDE DNQYRRKLAR EYKNSLANIP QIAFVEDVDG CESAQHLFQI
MVEDRDALMS HLQENEIFPG VHYRDNTEYK PYSYGFGTCP NAHRISEQVI SLPLHLHLES
DDIAHICETI RQFYIKNAF
//
