ID A0A0N0D9E8_9RHOB Unreviewed; 395 AA.
AC A0A0N0D9E8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=aspartate transaminase {ECO:0000256|ARBA:ARBA00012753};
DE EC=2.6.1.1 {ECO:0000256|ARBA:ARBA00012753};
GN Name=aspC_1 {ECO:0000313|EMBL:KPA22362.1};
GN ORFNames=shim_06400 {ECO:0000313|EMBL:KPA22362.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA22362.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA22362.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA22362.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:KPA22362.1}.
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; LAJH01000009; KPA22362.1; -; Genomic_DNA.
DR RefSeq; WP_054001172.1; NZ_LAJH01000009.1.
DR AlphaFoldDB; A0A0N0D9E8; -.
DR STRING; 1389006.shim_06400; -.
DR PATRIC; fig|1389006.3.peg.657; -.
DR OrthoDB; 9766084at2; -.
DR Proteomes; UP000037951; Unassembled WGS sequence.
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; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KPA22362.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037951};
KW Transferase {ECO:0000313|EMBL:KPA22362.1}.
FT DOMAIN 42..386
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 395 AA; 43306 MW; 037F7C77B54F2EC4 CRC64;
MTLSRTQATF APPVMEARRW LEGVTFTDAK PLINVSQAAP VDPPPAPLRA EIARVAQDVP
EAHLYGPVLG LPELRAEVAN HWSAAYGGPI GADQVAITSG CNQAFCASIS AIAGQGDEIL
LPTPWYFNHR MWLDMQGITT VPLVTGDSLL PDPKVAAALI TDRTRAIVLV TPNNPGGVEY
SADLVQAFFE LARDRDIKLI VDETYRDFDR RSEAPHALFS DPTWGDTLVQ LYSFSKAYRL
TGHRVGAMVA NAEFLAEAEK FLDTVTICPN QLGQYAALWG MQNLTQWLSG ERAEILDRRA
AISDNISTLS SQGWRLLGAG AYFAYVEHPF AMRSDDLAQA LVRDHHVLCL PGTMFMPADD
PAGGRQLRIA FANVNRAEIA VLFERLAQAD YAKRD
//
