ID A0A2T6B6D6_9RHOB Unreviewed; 457 AA.
AC A0A2T6B6D6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=L-2,4-diaminobutyrate transaminase {ECO:0000313|EMBL:PTX51618.1};
GN ORFNames=C8N34_103119 {ECO:0000313|EMBL:PTX51618.1};
OS Gemmobacter caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=589035 {ECO:0000313|EMBL:PTX51618.1, ECO:0000313|Proteomes:UP000244224};
RN [1] {ECO:0000313|EMBL:PTX51618.1, ECO:0000313|Proteomes:UP000244224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21823 {ECO:0000313|EMBL:PTX51618.1,
RC ECO:0000313|Proteomes:UP000244224};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PTX51618.1}.
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DR EMBL; QBKP01000003; PTX51618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6B6D6; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000244224; 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}.
SQ SEQUENCE 457 AA; 49209 MW; 565B7298C4CAD4D7 CRC64;
MADHDNELNA WDRDHFFHPS THMGMHARGE SARRVIAGGE GCHITDTAGK RSLDAFAGLY
CVNVGYGRTE IAEAIAEQAR ELAYYHAYVG HGTEASITLA RMIIERAPAH MSRVYFGLSG
SDANETNIKL IWYYNNILGR PEKKKIISRW RGYHGSGVMT GSLTGLSLFH AHFDLPRAPV
LHTEAPYFFR REDRSMTEAQ FSAHCAAKLE ELILSEGPDT IAAFIGEPIL GTGGIVPPPE
GYWAAIQAVL KKYDILLVAD EVVTGFGRLG TMFGSTHYGM EPDLITIAKG LTSAYAPLSG
SIVSDRLWQV LVQGSDDFGP MGHGWTYSAH PICAAAGVAN LRLIDDLSLV QNAGTIGAHF
RRGLADALAG HAHVGEVRGD GLMAAVEFVE DRDDRRFFDP ARKVGPAIAA ALLDRGVIGR
AMPQGDILGF APPLCLTEAE ADTVIAAAAD AVKSVLG
//