ID A0A2K6Q4M3_RHIRO Unreviewed; 482 AA.
AC A0A2K6Q4M3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:ENSRROP00000023735.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000023735.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000023735.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6Q4M3; -.
DR Ensembl; ENSRROT00000047943.1; ENSRROP00000023735.1; ENSRROG00000035697.1.
DR GeneTree; ENSGT00940000156125; -.
DR Proteomes; UP000233200; Unplaced.
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; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200}.
SQ SEQUENCE 482 AA; 53916 MW; E3D91D3E504AC532 CRC64;
MTLVWRHLLR PLCLVTSAPR ILEMHPFLSR ASWTSVTKLS LHTRPRMPSC DFMPERYQSL
GYNRVLEIHK EHLSPVVTAY FQKPLLLHQG HMEWLFDAEG NRYLDFFSGI VTVSVGHCHP
KVNAVAQKQL GRLWHTSTVF FHPPMHEYAE KLAALLPEPL KVIFLVNSGS EANELAMLMA
RAHSNNIDII SFRGAYHGGS PYTLGLTNVG TYKMELPGGT GCQPTMCPDV FRGPWGGSHC
RDSPVQTIRK CSCAPDCCQA KDQYIEQFKD TLSTSVAKSI AGFFAEPIQV QTGFGRLGSH
FWGFQTHDVL PDIVTMAKGI GNGFPMAAVV TTPEIAKSLA KRLQHFNTFG GNPMACAIGS
AVLEVIKEEN LQENSQEVGT YMLLKFAKLR DEFEIVGDVR GKGLMIGIEM VQDKISRRPL
PREEVNQIHE DCKHMGLLVG RGSIFSQTFR IAPSMCITKP EVDFATEVFR SALTQHMERR
AK
//
