ID A0A7K6U5W0_9AVES Unreviewed; 479 AA. AC A0A7K6U5W0; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 27-NOV-2024, entry version 12. DE RecName: Full=Alanine--glyoxylate aminotransferase 2, mitochondrial {ECO:0000256|ARBA:ARBA00039862}; DE EC=2.6.1.18 {ECO:0000256|ARBA:ARBA00044055}; 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-3-aminoisobutyrate-pyruvate aminotransferase {ECO:0000256|ARBA:ARBA00044258}; DE AltName: Full=D-AIBAT {ECO:0000256|ARBA:ARBA00041845}; DE AltName: Full=D-beta-aminoisobutyrate-pyruvate aminotransferase {ECO:0000256|ARBA:ARBA00044257}; 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; Neoaves; Strisores; 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: Multifunctional aminotransferase with a broad substrate CC specifcity. Catalyzes the conversion of glyoxylate to glycine using CC alanine as the amino donor. Catalyzes metabolism of not L- but the D- CC isomer of D-beta-aminoisobutyric acid to generate 2-methyl-3- CC oxopropanoate and alanine. Catalyzes the transfer of the amino group CC from beta-alanine to pyruvate to yield L-alanine and 3-oxopropanoate. CC Can metabolize NG-monomethyl-L-arginine (NMMA), asymmetric NG,NG- CC dimethyl-L-arginine (ADMA) and symmetric NG,N'G-dimethyl-L-arginine CC (SDMA). 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:ARBA00046156}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S)-2-aminobutanoate + glyoxylate = 2-oxobutanoate + glycine; CC Xref=Rhea:RHEA:77339, ChEBI:CHEBI:16763, ChEBI:CHEBI:36655, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:74359; CC Evidence={ECO:0000256|ARBA:ARBA00043679}; 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:ARBA00043726}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18394; CC Evidence={ECO:0000256|ARBA:ARBA00043726}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxobutanoate + L-alanine = (2S)-2-aminobutanoate + pyruvate; CC Xref=Rhea:RHEA:77355, ChEBI:CHEBI:15361, ChEBI:CHEBI:16763, CC ChEBI:CHEBI:57972, ChEBI:CHEBI:74359; EC=2.6.1.44; CC Evidence={ECO:0000256|ARBA:ARBA00043751}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N(omega)-dimethyl-L-arginine + 2-oxobutanoate = 5- CC (3,3-dimethylguanidino)-2-oxopentanoate + (2S)-2-aminobutanoate; CC Xref=Rhea:RHEA:77351, ChEBI:CHEBI:16763, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:74359, ChEBI:CHEBI:197301; CC Evidence={ECO:0000256|ARBA:ARBA00043779}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxohexanoate + N(omega),N(omega)-dimethyl-L-arginine = L-2- CC aminohexanoate + 5-(3,3-dimethylguanidino)-2-oxopentanoate; CC Xref=Rhea:RHEA:77363, ChEBI:CHEBI:35177, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:58455, ChEBI:CHEBI:197301; CC Evidence={ECO:0000256|ARBA:ARBA00043837}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxopentanoate + N(omega),N(omega)-dimethyl-L-arginine = 5- CC (3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminopentanoate; CC Xref=Rhea:RHEA:77359, ChEBI:CHEBI:28644, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:58441, ChEBI:CHEBI:197301; CC Evidence={ECO:0000256|ARBA:ARBA00043826}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate; CC Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190, CC ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18; CC Evidence={ECO:0000256|ARBA:ARBA00043825}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14079; CC Evidence={ECO:0000256|ARBA:ARBA00043825}; CC -!- CATALYTIC ACTIVITY: CC Reaction=oxaloacetate + L-alanine = L-aspartate + pyruvate; CC Xref=Rhea:RHEA:77347, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, CC ChEBI:CHEBI:29991, ChEBI:CHEBI:57972; CC Evidence={ECO:0000256|ARBA:ARBA00043764}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-ornithine + pyruvate = 5-amino-2-oxopentanoate + L-alanine; CC Xref=Rhea:RHEA:77327, ChEBI:CHEBI:15361, ChEBI:CHEBI:46911, CC ChEBI:CHEBI:57972, ChEBI:CHEBI:58802; CC Evidence={ECO:0000256|ARBA:ARBA00043777}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N('omega)-dimethyl-L-arginine + pyruvate = 5-(3,3'- CC dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77307, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:197308, CC ChEBI:CHEBI:197310; Evidence={ECO:0000256|ARBA:ARBA00043798}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N(omega)-dimethyl-L-arginine + oxaloacetate = 5-(3,3- CC dimethylguanidino)-2-oxopentanoate + L-aspartate; CC Xref=Rhea:RHEA:77343, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; CC Evidence={ECO:0000256|ARBA:ARBA00043749}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N(omega)-dimethyl-L-arginine + pyruvate = 5-(3,3- CC dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77303, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043669}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega)-methyl-L-arginine + pyruvate = 5-(3-methylguanidino)- CC 2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77319, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:57972, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314; CC Evidence={ECO:0000256|ARBA:ARBA00043758}; 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:ARBA00033660}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249; CC Evidence={ECO:0000256|ARBA:ARBA00033660}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-ornithine + glyoxylate = 5-amino-2-oxopentanoate + glycine; CC Xref=Rhea:RHEA:77331, ChEBI:CHEBI:36655, ChEBI:CHEBI:46911, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58802; CC Evidence={ECO:0000256|ARBA:ARBA00043808}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N('omega)-dimethyl-L-arginine + glyoxylate = 5-(3,3'- CC dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77315, CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:197308, CC ChEBI:CHEBI:197310; Evidence={ECO:0000256|ARBA:ARBA00043659}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N(omega)-dimethyl-L-arginine + glyoxylate = 5-(3,3- CC dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77311, CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043815}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega)-methyl-L-arginine + glyoxylate = 5-(3- CC methylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77323, CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:114953, CC ChEBI:CHEBI:197314; Evidence={ECO:0000256|ARBA:ARBA00043652}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; 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:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:TreeGrafter. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009436; P:glyoxylate catabolic process; IEA:TreeGrafter. DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; IEA:TreeGrafter. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000055; Alanine--glyoxylate aminotransferase 2, mitochondrial; 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; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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: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 //