ID G3RJK4_GORGO Unreviewed; 523 AA. AC G3RJK4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 65. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN Name=GPT2 {ECO:0000313|Ensembl:ENSGGOP00000015896.2}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000015896.2, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000015896.2, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000015896.2, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22398555; DOI=10.1038/nature10842; RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I., RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T., RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y., RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K., RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y., RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G., RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D., RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K., RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J., RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T., RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T., RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C., RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.; RT "Insights into hominid evolution from the gorilla genome sequence."; RL Nature 483:169-175(2012). RN [3] {ECO:0000313|Ensembl:ENSGGOP00000015896.2} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate; CC Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00024611}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase CC pathway; pyruvate from L-alanine: step 1/1. CC {ECO:0000256|ARBA:ARBA00025708}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. Alanine aminotransferase subfamily. CC {ECO:0000256|ARBA:ARBA00025785}. 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; CABD030100897; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030100898; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_004057650.1; XM_004057602.2. DR AlphaFoldDB; G3RJK4; -. DR SMR; G3RJK4; -. DR STRING; 9593.ENSGGOP00000015896; -. DR Ensembl; ENSGGOT00000016349.3; ENSGGOP00000015896.2; ENSGGOG00000016287.3. DR GeneID; 101142979; -. DR KEGG; ggo:101142979; -. DR CTD; 84706; -. DR eggNOG; KOG0258; Eukaryota. DR GeneTree; ENSGT00940000159061; -. DR HOGENOM; CLU_014254_3_1_1; -. DR InParanoid; G3RJK4; -. DR OMA; FGFECPP; -. DR OrthoDB; 5472891at2759; -. DR TreeFam; TF300839; -. DR UniPathway; UPA00528; UER00586. DR Proteomes; UP000001519; Chromosome 16. DR Bgee; ENSGGOG00000016287; Expressed in liver and 5 other cell types or tissues. DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd00609; AAT_like; 1. DR Gene3D; 1.10.287.1970; -; 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; IPR045088; ALAT1/2-like. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1. DR PANTHER; PTHR11751:SF311; ALANINE AMINOTRANSFERASE 2; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 111..510 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 523 AA; 57904 MW; 4DD87814C62C7DEA CRC64; MQRAAALVRR GCGPRTPSSW GRSQSSAAAE ASAVLKVRPE RSRRERILTL ESMNPQVKAV EYAVRGPIVL KAGEIELELQ RGIKKPFTEV IRANIGDAQA MGQQPITFLR QVMALCTYPN LLDSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAYITRR DGGVPADPDN IYLTTGASDG ISTILKILVS GGGKSRTGVM IPIPQYPLYS AVISELDAIQ VNYYLDEENC WALNVNELRR AVQEAKDHCD PKVLCIINPG NPTGQVQSRK CIEDVIHFAW EEKLFLLADE VYQDNVYSPD CRFHSFKKVL YEMGPEYSSN VELASFHSTS KGYMGECGYR GGYMEVINLH PEIKGQLVKL LSVRLCPPVS GQAAMDIVVN PPVAGEESFE QFSREKESVL GNLAKKAKLT EDLFNQVPGI HCNPLQGAMY AFPRIFIPAK AVEAAQAHQM APDMFYCMKL LEETGICVVP GSGFGQREGT YHFRMTILPP VEKLKTVLQK VKDFHINFLE KYA //