ID   A0A0Q7EG02_9CAUL        Unreviewed;       401 AA.
AC   A0A0Q7EG02;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=ASC65_04825 {ECO:0000313|EMBL:KQW83952.1};
OS   Brevundimonas sp. Root1279.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW83952.1, ECO:0000313|Proteomes:UP000050923};
RN   [1] {ECO:0000313|Proteomes:UP000050923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1279 {ECO:0000313|Proteomes:UP000050923};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW83952.1, ECO:0000313|Proteomes:UP000050923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1279 {ECO:0000313|EMBL:KQW83952.1,
RC   ECO:0000313|Proteomes:UP000050923};
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   -!- 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:KQW83952.1}.
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DR   EMBL; LMEB01000004; KQW83952.1; -; Genomic_DNA.
DR   RefSeq; WP_056450045.1; NZ_LMEB01000004.1.
DR   AlphaFoldDB; A0A0Q7EG02; -.
DR   STRING; 1736443.ASC65_04825; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000050923; 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:KQW83952.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050923};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KQW83952.1}.
FT   DOMAIN          33..393
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   401 AA;  42964 MW;  DEEB6FB449A2EB1E CRC64;
     MSSLQSSALA RVKPSATLAV TAQARQLKAE GRDVIGLGAG EPDFDTPENI KEAAIAAIRR
     GETKYTDADG MPELKAAISA KFKRENGLDY APAQIHVAPG GKPVIFNALV ATLNPGDEVI
     VPAPYWVSYP DMVLLAGGEP VTVIGEEKDG FKLLPAVLEA AITPRTRWLI LNSPSNPTGA
     AYTRAELEGL ADVLRRHPHV WVLTDDMYEH LVYGDFEYTT IAQVAPDLID RTLTVNGVSK
     AYAMTGWRIG YAGGPKPLID LMRKVASQTT SNPTSISQWA AVEALNGPQD FMAERRAAFE
     KRRDLVVSML NQTAGVTCAT PEGAFYVYPS IAGLIGKATE SGVVIDGDST FAAELLNAEG
     VAVVQGEAFG LSPYFRISYA TSETVLEEAC ARIQRFCAGL R
//