ID A0A0Q5YT13_9BURK Unreviewed; 494 AA.
AC A0A0Q5YT13;
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 {ECO:0000313|EMBL:KQT08801.1};
GN ORFNames=ASG30_15055 {ECO:0000313|EMBL:KQT08801.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT08801.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT08801.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT08801.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT08801.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT08801.1,
RC ECO:0000313|Proteomes:UP000051173};
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, 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:KQT08801.1}.
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DR EMBL; LMQL01000013; KQT08801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5YT13; -.
DR STRING; 1736365.ASG30_15055; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000051173; 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; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51371; CBS; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KQT08801.1};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000051173};
KW Transferase {ECO:0000313|EMBL:KQT08801.1}.
FT DOMAIN 62..122
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 494 AA; 53493 MW; E008B97AD3F95079 CRC64;
MRLRVPLSLT WKDAVQRMDR EGEGILLAVD GQGALRRTVT DGDLRRALLA SAAPGSTLAD
LPSNPPISVG EDADATAVRQ LMEQHRISHV PVVDAQGRPV DLIHSRELAG RIWLSSPHLG
EEETVFVEEA FRTNWIAPLG PHVDGFEREV AAFTGVGHAA ALSSGTAAIH LGLLLLGVQP
GDTVFCSSLT FVGSCNPILY CGARPVFIDS EPGSWNMSPA ALERAFEWAR RENRMPRCVV
LVNLYGQSAD MDALLPICRR HGVPVLEDAA ESLGARYKDR ASGSFGDVGV FSFNGNKIIT
TSGGGMLVSD DAALIARARK LATQAREPAA HYEHREVGFN YRMSNVLAGI GRGQLKVLPQ
RVQRRREVFE TYRQAFEGVD GLAWMPEPAG SLSTRWLTCG VLHGPGAQAR RDAVLRRLER
HAIEARPVWK PMHLQPLYAQ APYFEHEPGT DVSAGLFEAG LCLPSGSNLS AAQLDRVVDH
LRHALAAGAS DALA
//
