UniProt: A0A2K6MWN1

Database: UniProt
Entry: A0A2K6MWN1_RHIBE

LinkDB:  A0A2K6MWN1_RHIBE 
Original site:  A0A2K6MWN1_RHIBE

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (8)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (1)   
All databases (19)   

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ID   A0A2K6MWN1_RHIBE        Unreviewed;       430 AA.
AC   A0A2K6MWN1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000040170.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000040170.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000040170.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC       metabolite L-kynurenine to form kynurenic acid (KA). As a member of the
CC       malate-aspartate shuttle, it has a key role in the intracellular NAD(H)
CC       redox balance. Is important for metabolite exchange between
CC       mitochondria and cytosol, and for amino acid metabolism. Facilitates
CC       cellular uptake of long-chain free fatty acids.
CC       {ECO:0000256|ARBA:ARBA00037556}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC         glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC         ChEBI:CHEBI:58454; EC=2.6.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00036795};
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   RefSeq; XP_017734448.1; XM_017878959.1.
DR   AlphaFoldDB; A0A2K6MWN1; -.
DR   STRING; 61621.ENSRBIP00000040170; -.
DR   Ensembl; ENSRBIT00000064200.1; ENSRBIP00000040170.1; ENSRBIG00000043519.1.
DR   GeneID; 108533911; -.
DR   KEGG; rbb:108533911; -.
DR   CTD; 2806; -.
DR   GeneTree; ENSGT00950000183082; -.
DR   OMA; VGACTIV; -.
DR   OrthoDB; 1123851at2759; -.
DR   Proteomes; UP000233180; Unplaced.
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   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000480};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Transferase {ECO:0000256|RuleBase:RU000480}.
FT   DOMAIN          58..425
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   430 AA;  47400 MW;  6350906B99492A4D CRC64;
     MALLHSGRVL SGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
     NLGVGAYRDD SGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSDV
     LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR
     YYDPKTCGFD FTGAMEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA
     FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE
     AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKGMADR IIGMRTQLVS
     NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVGY
     LAHAIHQVTK
//

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