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Database: UniProt
Entry: X6KUE1_9RHOB
LinkDB: X6KUE1_9RHOB
Original site: X6KUE1_9RHOB 
ID   X6KUE1_9RHOB            Unreviewed;       464 AA.
AC   X6KUE1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 2.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Contig2, whole genome shotgun sequence {ECO:0000313|EMBL:ETA50317.2};
GN   ORFNames=P279_20095 {ECO:0000313|EMBL:ETA50317.2};
OS   Rhodobacteraceae bacterium PD-2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA50317.2, ECO:0000313|Proteomes:UP000023196};
RN   [1] {ECO:0000313|EMBL:ETA50317.2, ECO:0000313|Proteomes:UP000023196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD-2 {ECO:0000313|EMBL:ETA50317.2,
RC   ECO:0000313|Proteomes:UP000023196};
RX   PubMed=25700405;
RA   Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT   "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT   Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT   Prorocentrum donghaiense.";
RL   Genome Announc. Announc.3:e01549-14(2015).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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:ETA50317.2}.
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DR   EMBL; AWRV02000002; ETA50317.2; -; Genomic_DNA.
DR   AlphaFoldDB; X6KUE1; -.
DR   HOGENOM; CLU_016922_4_1_5; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000023196; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023196}.
SQ   SEQUENCE   464 AA;  50531 MW;  9C61B9EE9F5B12E9 CRC64;
     MTHLTPNSPT AELQALDAAH HMHPFTHGQE LGAKGARVIT RAEGCWLTDS DGNRILDAMA
     GLWCVNVGYG RKELAEVAAR QMQELPFYNT FFQTTHVPAL NLAAKLAELV PGDLNHVFFA
     GSGSEANDTN LRMVRTYWAE KGQPQRDVII SRWNAYHGSS VGSGSLGGMK GIHMQGGLPI
     PGVHHIDQPN WWAEGGYSTP EAFGLERAQA LEAAILEIGP DRVAAFIAEP VQGAGGVIVP
     PETYWPEVQK IVDKYGILLI ADEVICGFGR TGEWFGSQTM GIRPDIMTIA KGLSSGYIPI
     GGSIVSDEVA SVIGNTEFNH GYTYSGHPVA CAVALENLRI IEEEKLVEKV RDDTGVYLRE
     RFETLTDHPM VGEAKIVGMM GSIALTPQKE TRAPFKAEAG TVGFKVRERC FANNLIMRHV
     GDRMIISPPL VISREEIDTL IERAWQSLDE GYAAVKAEGL FEPA
//
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