ID R4G4U0_RHOPR Unreviewed; 422 AA.
AC R4G4U0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EMBL:JAA77039.1};
RN [1] {ECO:0000313|EMBL:JAA77039.1}
RP NUCLEOTIDE SEQUENCE.
RA Ribeiro J.M.C., Genta F.A., Sorgine M.H.F., Paiva-Silva G.O.,
RA Majerowicz D., Medeiros M., Koerich L., Terra W.R., Ferreira C.,
RA Pimentel A.C., Bisch P.M., Diniz M.M.P., Nascimento R., Salmon D.,
RA Silber A.M., Alves M., Oliveira M.F., Gondim K.C., Silva Neto M.A.C.,
RA Atella G.C., Araujo H., Dias F.S., Polycarpo C.R., Fampa P., Melo A.C.,
RA Tanaka A.S., Balczun C., Oliveira J.H.M., Goncalves R., Lazoski C.,
RA Pereira M.A., Rivera-Pomar R., Diambra L., Schaub G.A., Garcia E.S.,
RA Azambuja P., Braz G.R.C., Oliveira P.L.;
RT "An insight into the transcriptome of the digestive tract of the blood
RT sucking bug, Rhodnius prolixus.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:RPRC009777-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
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 ECO:0000256|RuleBase:RU000480};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU000480}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; ACPB03008949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GAHY01000471; JAA77039.1; -; mRNA.
DR AlphaFoldDB; R4G4U0; -.
DR STRING; 13249.R4G4U0; -.
DR EnsemblMetazoa; RPRC009777-RA; RPRC009777-PA; RPRC009777.
DR VEuPathDB; VectorBase:RPRC009777; -.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; R4G4U0; -.
DR OMA; VGACTIV; -.
DR OrthoDB; 1123851at2759; -.
DR Proteomes; UP000015103; 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:0006520; P:amino acid metabolic process; 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; IPR000796; Asp_trans.
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; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase {ECO:0000256|RuleBase:RU000480,
KW ECO:0000313|EMBL:JAA77039.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW Transferase {ECO:0000256|RuleBase:RU000480, ECO:0000313|EMBL:JAA77039.1}.
FT DOMAIN 50..416
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 422 AA; 46844 MW; 7C6BBE7B4A9E5A9C CRC64;
MLVKFSKLLK AATNCSHFSK SASWWSKVEM GPPDAILGVT EAFKRDTNPQ KINLGVGAYR
DDNGKPYVLP SVIQAEEQIM SEHLDKEYAA IHGIQEFCAK SAALALGDDS PIIKNGLNAT
VQSLSGTGAL RLGAAFLQKF FPGNKEVYVP DPTWGNHIPI FNHSGLPIKK YRYYDPKTVG
FDFNGALEDL SKIPEKSIIL LHACAHNPTG IDPKKEQWKE LSAIIKKKNH FPFFDMAYQG
FASGDVANDA FALRYFLNEG HQVVLAQSYA KNLGLYGERI GAFTVVASSS EEAAKVMSQI
KILIRPMYSN PPIHGARIVT KILSDPKLKN QWLSEVKGMA DRIISIRAKL KSQLAAEGTT
KNWNHITDQI GMFCYTGINP KQVERLTKEF NVYLTKDGRI SMAGVTTKNY KHLAHAMHQV
TK
//
