ID M3YUL2_MUSPF Unreviewed; 516 AA.
AC M3YUL2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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};
GN Name=AGXT2 {ECO:0000313|Ensembl:ENSMPUP00000015022.1,
GN ECO:0000313|RefSeq:XP_004738095.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015022.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000015022.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004738095.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004738095.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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=2-oxobutanoate + N(omega),N(omega)-dimethyl-L-arginine = (2S)-
CC 2-aminobutanoate + 5-(3,3-dimethylguanidino)-2-oxopentanoate;
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 = 5-
CC (3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminohexanoate;
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=L-alanine + oxaloacetate = 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=glyoxylate + L-ornithine = 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=glyoxylate + N(omega),N('omega)-dimethyl-L-arginine = 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=glyoxylate + N(omega),N(omega)-dimethyl-L-arginine = 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=glyoxylate + N(omega)-methyl-L-arginine = 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}.
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DR EMBL; AEYP01001469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01001470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004738095.1; XM_004738038.2.
DR STRING; 9669.ENSMPUP00000015022; -.
DR Ensembl; ENSMPUT00000015259.1; ENSMPUP00000015022.1; ENSMPUG00000015131.1.
DR GeneID; 101688685; -.
DR KEGG; mpuf:101688685; -.
DR CTD; 64902; -.
DR eggNOG; KOG1404; Eukaryota.
DR GeneTree; ENSGT00940000156125; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR OMA; MVPGFKY; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; IEA:Ensembl.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IEA:Ensembl.
DR GO; GO:0009436; P:glyoxylate catabolic process; IEA:Ensembl.
DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
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; 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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|RefSeq:XP_004738095.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Transferase {ECO:0000313|RefSeq:XP_004738095.1}.
SQ SEQUENCE 516 AA; 57480 MW; 0E57CCED96C14FBD CRC64;
MTPAWRHLLR AWYLQTSSSR IPKMCPSLSR AFRTSVTKLG LHTKHRMPPC DFTPEKYQSL
AYERVLEIHS QHLAPMSTAY FPKPLLLHQG HMEWLFDYEG NRYLDFFSGI VTVSVGHCHP
KVNAVAQKQL GRLWHTSSLF FHSPIHEFAE KLSALLPEPL KVIFLVNSGS EANDLAMLMA
RAHSNSTDII SFRGGYHGCS PYTLGLTNVG PYKMELPSGT GCQSTMCPDV FRGPWGGSHC
RDSPVQTIRK CSCAPDCCQA KDQYIEQFKD TLNTSVAKSI AGFFAEPIQG VNGVVQYPKG
FLQEAFELVR ERGGVCIADE VQTGFGRLGS HFWGFQTHGI LPDIVTMAKG IGNGFPMAAV
VTTPEIAKSL ATRLFHFNTF GGNPMACAIG SAVLEVIKEE KLQENSHDVG TYMLQKFAEL
RDEFEIVGDV RGKGLMIGIE MVKDKVSCQP LPREEVNEIH DDCKRMGLLI GRGGIFAQTF
RVAPSMCITK PDVHFAVEVF RSALIQHMER RAKSNF
//
