ID A0A0X3TKJ5_9RHOB Unreviewed; 388 AA.
AC A0A0X3TKJ5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=AVO45_13230 {ECO:0000313|EMBL:KUJ76264.1};
OS Ruegeria marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ76264.1, ECO:0000313|Proteomes:UP000053791};
RN [1] {ECO:0000313|EMBL:KUJ76264.1, ECO:0000313|Proteomes:UP000053791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ76264.1,
RC ECO:0000313|Proteomes:UP000053791};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000984};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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:KUJ76264.1}.
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DR EMBL; LQBQ01000036; KUJ76264.1; -; Genomic_DNA.
DR RefSeq; WP_068349150.1; NZ_LQBQ01000036.1.
DR AlphaFoldDB; A0A0X3TKJ5; -.
DR STRING; 1685379.AVO45_13230; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000053791; Unassembled WGS sequence.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:KUJ76264.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053791};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KUJ76264.1}.
FT DOMAIN 40..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 388 AA; 41018 MW; 30AF447CB034FB2B CRC64;
MTIQNGLGGF RRAGRLDGIE LSEIVQISER AAQLRAQGVD VIALSTGEPD FPTPPHVVEA
AHKAALDGQT RYPATAGTPA LRSAIAEQAG VESAQVIVST GAKQVLVGAF LATLDPGDQV
ITTAPFWTSY ADMVKLAGGV PIVLNCPRKQ GFKLTPEQLE AAITPRTRWL LLNTPSNPTG
AVYTEAELRA LGAVLERHRQ VWVISDEIYQ HLAYAPFTPF TQAVPTLADR TLTVNGVSKA
YSMTGWRIGW GIGPAPLIKA MAAVQGQITS GACSIAQAAA LAALTGPQDL LAERRAAMRA
RRDLVVAGLN AAGLACPVPD GAFYVFPQTP QAMPSDPAFC RHLLDHAGVA VVPGRAFGMP
GHFRLSFAYD TDSLTQGLRR IADATAKL
//
