ID A0A0M7BCF6_9RHOB Unreviewed; 400 AA.
AC A0A0M7BCF6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=JSE7799_02790 {ECO:0000313|EMBL:CUH40061.1};
OS Jannaschia seosinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH40061.1, ECO:0000313|Proteomes:UP000049455};
RN [1] {ECO:0000313|EMBL:CUH40061.1, ECO:0000313|Proteomes:UP000049455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH40061.1,
RC ECO:0000313|Proteomes:UP000049455};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-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}.
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DR EMBL; CYPR01000186; CUH40061.1; -; Genomic_DNA.
DR RefSeq; WP_055664166.1; NZ_CYPR01000186.1.
DR AlphaFoldDB; A0A0M7BCF6; -.
DR STRING; 313367.JSE7799_02790; -.
DR OrthoDB; 9766084at2; -.
DR Proteomes; UP000049455; 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:CUH40061.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049455};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:CUH40061.1}.
FT DOMAIN 32..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 400 AA; 42993 MW; BDE239D799BFC366 CRC64;
MAFLSDMLAR VKPSPTIAVT NKARELKAAG RDVIGLGAGE PDFDTPQNIK DAATRAIAEG
KTKYTAVDGI PELKQAIRDK FLRDNGLDYT PAQISVGTGG KQVLYNAFVA TLNPSDEVVI
PAPYWVSYPD MVLLAGGVPV VAEAGIETGF KLSPEALEAA ITDRTKWFIF NSPSNPTGAG
YTEEELRGLT DVLLRHPHVW VLTDDMYEHL VFDGFTFVTP AQVEPRLKDR TLTVNGVSKA
YSMTGWRIGY AGGPEELIAA MRKVQSQSTS NPCSISQWAA VEALNGPQDF IGSNNAAFRR
RRDLVVAGLN DCPGIICPVP EGAFYVYPSI AGCIGKVTVG GARIDDDEAF ATALLDEEGV
AVVFGSAFGL SPHFRVSYAT SDDSLAEACS RIRRFCEALS
//
