ID A0A270BMD7_9SPHN Unreviewed; 438 AA.
AC A0A270BMD7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:PAL25326.1};
DE EC=2.6.1.18 {ECO:0000313|EMBL:PAL25326.1};
GN ORFNames=CD928_02205 {ECO:0000313|EMBL:PAL25326.1};
OS Sphingopyxis sp. GW247-27LB.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=2012632 {ECO:0000313|EMBL:PAL25326.1, ECO:0000313|Proteomes:UP000216381};
RN [1] {ECO:0000313|Proteomes:UP000216381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW247-27LB {ECO:0000313|Proteomes:UP000216381};
RA Ray J., Price M.N., Deutschbauer A.M.;
RL Submitted (JUN-2017) 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:PAL25326.1}.
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DR EMBL; NIWD01000002; PAL25326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A270BMD7; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000216381; Unassembled WGS sequence.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:PAL25326.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PAL25326.1}.
SQ SEQUENCE 438 AA; 46462 MW; 83D5B375F9D0B0E2 CRC64;
MKGENDPLAA FWMPFTANRA FKAHPRQLVS ASGMHYRSAD GRTILDGTAG LWCSNAGHCR
PEIAEAIAKA AASLDFAPTF QLGHPQAFEL AQRLAALMPE GLDRIFFTNS GSESVDTALK
IALAIQRARG QGTRTRLIGR ERGYHGVGFG GISVGGIVSN RRTFGGGLPG ADHLRHTHDI
ARNAFSRGFP PHGAELADDL QRLVDLHGAE TIAAVIVEPM AGSTGVLLPP AGYLQRLREI
CDRHGILLIF DEVITAFGRV GGATAAGRWG VTPDILTMAK GLTNAAVPMG AVAVKRELHD
AVIDSAPGGI ELFHGYTYSG HPLACAAGLA ALDLYARDGL FDRADELAGY WEDAAHGLKG
RRHVIDIRTI GLVAGIELEP RPGAPTARAM ELFHACFDNG LLVRATGDII ALSPPLIVEK
AEIDAMFGTL GELIETIA
//
