ID A0A7K6U5W0_9AVES Unreviewed; 479 AA. AC A0A7K6U5W0; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 24-JAN-2024, entry version 8. DE RecName: Full=Alanine--glyoxylate aminotransferase 2, mitochondrial {ECO:0000256|ARBA:ARBA00039862}; DE EC=2.6.1.40 {ECO:0000256|ARBA:ARBA00039130}; DE EC=2.6.1.44 {ECO:0000256|ARBA:ARBA00013049}; DE AltName: Full=(R)-3-amino-2-methylpropionate--pyruvate transaminase {ECO:0000256|ARBA:ARBA00041662}; DE AltName: Full=Beta-ALAAT II {ECO:0000256|ARBA:ARBA00042611}; DE AltName: Full=Beta-alanine-pyruvate aminotransferase {ECO:0000256|ARBA:ARBA00042669}; DE AltName: Full=D-AIBAT {ECO:0000256|ARBA:ARBA00041845}; DE Flags: Fragment; GN Name=Agxt2 {ECO:0000313|EMBL:NWX18201.1}; GN ORFNames=AEGBEN_R12663 {ECO:0000313|EMBL:NWX18201.1}; OS Aegotheles bennettii. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes; OC Aegothelidae; Aegotheles. OX NCBI_TaxID=48278 {ECO:0000313|EMBL:NWX18201.1, ECO:0000313|Proteomes:UP000559068}; RN [1] {ECO:0000313|EMBL:NWX18201.1, ECO:0000313|Proteomes:UP000559068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-DU-029-76 {ECO:0000313|EMBL:NWX18201.1}; RC TISSUE=Heart {ECO:0000313|EMBL:NWX18201.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Can metabolize asymmetric dimethylarginine (ADMA) via CC transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid CC (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and CC this activity provides mechanism through which the kidney regulates CC blood pressure. {ECO:0000256|ARBA:ARBA00037030}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3- CC oxopropanoate + L-alanine; Xref=Rhea:RHEA:18393, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57731, ChEBI:CHEBI:57972; EC=2.6.1.40; CC Evidence={ECO:0000256|ARBA:ARBA00035890}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glyoxylate + L-alanine = glycine + pyruvate; CC Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44; CC Evidence={ECO:0000256|ARBA:ARBA00001781}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954, CC ECO:0000256|RuleBase:RU003560}. 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:NWX18201.1}. 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; VZRW01007452; NWX18201.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7K6U5W0; -. DR Proteomes; UP000559068; Unassembled WGS sequence. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR45688; -; 1. DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, KW ECO:0000313|EMBL:NWX18201.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU003560}; KW Reference proteome {ECO:0000313|Proteomes:UP000559068}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:NWX18201.1}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NWX18201.1" FT NON_TER 479 FT /evidence="ECO:0000313|EMBL:NWX18201.1" SQ SEQUENCE 479 AA; 53386 MW; 8694A297FE8AC88A CRC64; RQQKWKSPIS TQAKMPPCDF VPEKYTSYPY KRIQKIREQN IAPSLRTYYK KPLLLHQGHM QWLFDYEGRR YLDLFAGIVT VGVGHCHPKV TMATQKQLAR LWHTTNIYLH PSIHEYAEKL TSLLPDPLKV VYLTNSGTEA NDLAMFMARL YTRNFDMISL RGAYHGGSAS TLGLTSIGLY KHGVASGFGC STTMLPDVFR GPWGGSRCRD SPVQTVRKCS CSEGVCHANN QYIEQLKDTL STLMPKTIAG FIAEPIQGVN GAVQYPRNFL KEAFRLVRER GGVCISDEVQ TGFGRTGSHF WGFQTHGVVP DIVTLAKAIG NGFPMAAVIT TKEIASSLNQ NLHFNTFGGS PLACVVGSAV LDVIKEDNLQ KNSEDVGTYM LLELAKLRDK FEIVGDVRGK GLMIGVEMVT DKDSRHPLPP EEMSQIWEDC KDMGVLIGKG GLYGQTFRIK PPMCITKKDV DFAVEVFHTA LQRHVEKTA //