ID A0A0R2TQQ6_9RHOB Unreviewed; 397 AA.
AC A0A0R2TQQ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:KRO89176.1};
GN ORFNames=ABR89_10545 {ECO:0000313|EMBL:KRO89176.1};
OS Rhodobacter sp. BACL10 MAG-120910-bin24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1655597 {ECO:0000313|EMBL:KRO89176.1, ECO:0000313|Proteomes:UP000051243};
RN [1] {ECO:0000313|EMBL:KRO89176.1, ECO:0000313|Proteomes:UP000051243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL7 MAG-120910-bin24 {ECO:0000313|EMBL:KRO89176.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRO89176.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LICH01000035; KRO89176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TQQ6; -.
DR Proteomes; UP000051243; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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:KRO89176.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:KRO89176.1}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 397 AA; 43153 MW; 95529D439C52D1B0 CRC64;
MTAAPNVYDA EPIPAEARAE IDRLLASGDL FRYTRPQDAP VALLEQEFAA LLGAKYALAV
SSCSAALFLS LKALNLPHEA RVLIPAFTFA AVPSAVVHAD CVPVLVEVGE NYRINMEDFA
GKLDGSIKAV LISHMRGHTS DMDPIMALCT AHNVPLLEDA AHSLGTTWHN RQIGTLGKIG
CFSFQSYKLV NAGEGGILIT DDPDLLARAV IMSGAYEENW QKHQGLAEHF AKWQNHLPLY
NLRMQNLSAA VIRPQLPLVA SRVSQGLANH DYVAGLLNAC PVLTVPKPLS PEARAPDSIQ
FNLPQDWTDA QALGFQTRAM ADGVKVQIFG LSQGNARAYW NWKFLAPQPD LPQTRKMLMR
AADMRLPARL TCADLDYIAS TLIKAAMITA QAPLAAK
//
