ID A0A0Q8R0E7_9BURK Unreviewed; 367 AA.
AC A0A0Q8R0E7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KRB91437.1};
GN ORFNames=ASE07_16400 {ECO:0000313|EMBL:KRB91437.1};
OS Noviherbaspirillum sp. Root189.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB91437.1, ECO:0000313|Proteomes:UP000051303};
RN [1] {ECO:0000313|EMBL:KRB91437.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB91437.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB91437.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB91437.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRB91437.1}.
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DR EMBL; LMHZ01000009; KRB91437.1; -; Genomic_DNA.
DR RefSeq; WP_057290002.1; NZ_LMHZ01000009.1.
DR AlphaFoldDB; A0A0Q8R0E7; -.
DR STRING; 1736487.ASE07_16400; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000051303; 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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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:KRB91437.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000051303};
KW Transferase {ECO:0000313|EMBL:KRB91437.1}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 367 AA; 40172 MW; 88B1E3284946246A CRC64;
MEFIDLRTQY NEMRYEIGAR IQTVLDHGSY IMGPEVKELE QRLAAYTGAT HCITVSSGTE
ALLIALMAIG IQPGDEVITT PFSFVATAEV IVMLGAIPVF VDIEAETCLI DVSRIEQAIT
SKTRAIIPVS LYGQPADMDE INAIAEQHGM VVIEDAAQSF GATYKGHRSC NLSAIACTSF
FPSKPLGCYG DGGAIFTSNS ALAQAMREIR VHGQSQRYVH TRIGVGGRMD TMQCAVVLAK
FDYFDWEVEQ RMRLAARYDQ LLSGHIDVIR QRSNRTSVYA QYTISLDNRA VVEALLKQQG
IPTAVHYPIP IPMQAAYARF CPNPHFPISM IMARKVMSLP MGPYLKPDDL SRVADAVLLA
AGAGPTG
//
