ID A0A0B4C2H3_9RHOB Unreviewed; 392 AA.
AC A0A0B4C2H3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:KIC50737.1};
GN ORFNames=RA29_02045 {ECO:0000313|EMBL:KIC50737.1};
OS Tateyamaria sp. ANG-S1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tateyamaria.
OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC50737.1, ECO:0000313|Proteomes:UP000031171};
RN [1] {ECO:0000313|Proteomes:UP000031171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC50737.1}.
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DR EMBL; JWLL01000003; KIC50737.1; -; Genomic_DNA.
DR RefSeq; WP_039682513.1; NZ_JWLL01000003.1.
DR AlphaFoldDB; A0A0B4C2H3; -.
DR STRING; 1577905.RA29_02045; -.
DR OrthoDB; 9768668at2; -.
DR Proteomes; UP000031171; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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: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:KIC50737.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000031171};
KW Transferase {ECO:0000313|EMBL:KIC50737.1}.
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 392 AA; 42667 MW; 0D8F707E04A9EB45 CRC64;
MTLPDMHSAE PIPAAARAEI DRLLTSGDLF RYTAPQDAPV SLLEAEFAEM MGSKFALAVS
SCSAALFLSL KALDLPRDAR VLIPGFTFAA VPSSVLHADC LPVLCEVRDD YRIDIDDFVA
KLPTVQAVII SHMRGHTSDM DAIMTLCRAA HVPVIEDAAH SLGTLWNGQK IGTIGTIGCF
SFQSYKMINA GEGGIMITDD ADLVARAIIM SGAYEHNWKK HPVLQDAFAR HQNQWPLYNL
RMSNLSAAVI RPQLPHLAKR VEDGRRNHDH VAALLERSAH IHVPDPLAGE IRAPDSIQFN
LVDMTDAQVD AFVAAAATRG VKVQVFGASA DNARAFWNWQ FIPNLPDLPQ TRAMLMRACD
VRLPVHLPTD TLDAVADALC DAVATATEPR AA
//
