ID A0A0Q5ZZI5_9BRAD Unreviewed; 442 AA.
AC A0A0Q5ZZI5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Beta alanine--pyruvate aminotransferase {ECO:0000313|EMBL:KQT23472.1};
GN ORFNames=ASG57_23740 {ECO:0000313|EMBL:KQT23472.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT23472.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT23472.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT23472.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT23472.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT23472.1,
RC ECO:0000313|Proteomes:UP000051536};
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 class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {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:KQT23472.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMQJ01000008; KQT23472.1; -; Genomic_DNA.
DR RefSeq; WP_024341724.1; NZ_LMQJ01000008.1.
DR AlphaFoldDB; A0A0Q5ZZI5; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000051536; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF1; BETA-ALANINE--PYRUVATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:KQT23472.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:KQT23472.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQT23472.1}.
SQ SEQUENCE 442 AA; 47736 MW; 30A77C152206FC84 CRC64;
MTLHQIPNTI KTDSYWMPFT ANRQFKKSPR LFSSAEGMYY TSVDGRQVID GSAGLWCVNA
GHGRKQIAAA VERQLMTLDF APSFQMGHPL AFDFAERLAE IAPKGLDRVF FTNSGSESVD
TALKIALAYH RANGQASRTR LIGRERGYHG VGFGGTSVGG MVANRRAFTT LLPGVDHIRH
THDLTRNAFA KDLPEHGAEL ADDLERLVAL HGAETIAAVI VEPVPGSTAV LPPPKGYLKR
LREICDKHGI LLIFDEVITG FGRLGTPFAA NFFGVTPDLM TTAKGITNGT VPCGAVFASR
KVYDGMMTGP ENQIELFHGY TYSAHPVACA AGIATLDIYK DEGLLTRGAS LAEYWRDALH
SLKGLPNVVD IRNCGLMGAV ELAPRDGVVG ARGYDMLVEC FNSGLYLRTG GDSVAMSPPL
IVEKSHIDKM VSILGDAIKK VA
//
