ID B3CTD1_ORITI Unreviewed; 400 AA.
AC B3CTD1;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aatA {ECO:0000313|EMBL:BAG40628.1};
GN OrderedLocusNames=OTT_1170 {ECO:0000313|EMBL:BAG40628.1};
OS Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=334380 {ECO:0000313|EMBL:BAG40628.1, ECO:0000313|Proteomes:UP000001033};
RN [1] {ECO:0000313|Proteomes:UP000001033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ikeda {ECO:0000313|Proteomes:UP000001033};
RX PubMed=18508905; DOI=10.1093/dnares/dsn011;
RA Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M., Fukuhara M.,
RA Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T., Oshima K.,
RA Tamura A., Hattori M., Hayashi T.;
RT "The whole-genome sequencing of the obligate intracellular bacterium
RT Orientia tsutsugamushi revealed massive gene amplification during reductive
RT genome evolution.";
RL DNA Res. 15:185-199(2008).
CC -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC oxoglutarate to glutamate and oxaloacetate. Can also transaminate
CC prephenate in the presence of glutamate.
CC {ECO:0000256|ARBA:ARBA00002385}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-arogenate = L-glutamate + prephenate;
CC Xref=Rhea:RHEA:22880, ChEBI:CHEBI:16810, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58180; EC=2.6.1.79;
CC Evidence={ECO:0000256|ARBA:ARBA00000771};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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; AP008981; BAG40628.1; -; Genomic_DNA.
DR RefSeq; WP_012461697.1; NC_010793.1.
DR AlphaFoldDB; B3CTD1; -.
DR GeneID; 66653176; -.
DR KEGG; ott:OTT_1170; -.
DR HOGENOM; CLU_017584_4_3_5; -.
DR OrthoDB; 9804407at2; -.
DR Proteomes; UP000001033; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033854; F:glutamate-prephenate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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 PRINTS; PR00753; ACCSYNTHASE.
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:BAG40628.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:BAG40628.1}.
FT DOMAIN 32..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 400 AA; 44235 MW; 7D364934EF2A3739 CRC64;
MSLITHRINR IKSSPTLAVA KKAAELQQQG KNIISLSVGE LNFDTHDNIK AQAIEAINRG
MTKYTNVDGM PELKQAVKNK FKVENNLDYQ LDELIVSSGA KQVIFNALLA TLDIGDEVII
PTPYWVSYPD IVSLTGATSK FIYCHESSNF KITPAQLSNA ITDKTKWLLL NSPNNPTGAI
YTIEELKLLA EILSIHKNIH IMCDDIYEHI IFDNNKFYTL AAIAPSLKER IFIVNGVSKA
YAMTGWRIGY GAGNSEIIKA MIKIQSHSTS NPCSISQVAA IEALTGSQSH IQDNITILQR
NRDLAFNILN NTIGLKCYKP TGTFYLFVSC QELLHKATST GQKINTSNDF ACYLLEEAEV
SVVPGEAFGI NGYFRLSYAV DAAELNIACL QIKKACEKLI
//
