ID G1SNJ7_RABIT Unreviewed; 517 AA.
AC G1SNJ7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 66.
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:ENSOCUP00000004564.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000004564.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000004564.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000004564.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000004564.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004564.3};
RG Ensembl;
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; AAGW02030398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002714151.1; XM_002714105.3.
DR AlphaFoldDB; G1SNJ7; -.
DR SMR; G1SNJ7; -.
DR STRING; 9986.ENSOCUP00000004564; -.
DR PaxDb; 9986-ENSOCUP00000004564; -.
DR Ensembl; ENSOCUT00000005265.4; ENSOCUP00000004564.3; ENSOCUG00000005264.4.
DR GeneID; 100352336; -.
DR KEGG; ocu:100352336; -.
DR CTD; 64902; -.
DR eggNOG; KOG1404; Eukaryota.
DR GeneTree; ENSGT00940000156125; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; G1SNJ7; -.
DR OMA; MVPGFKY; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000001811; Chromosome 11.
DR Bgee; ENSOCUG00000005264; Expressed in adult mammalian kidney and 10 other cell types or tissues.
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 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
SQ SEQUENCE 517 AA; 57453 MW; CFE6F2603C6419E2 CRC64;
MTLYWRHLQR ALRQEASFPR IPKTCPVLSL GASWTSVAKL SLHTKPKMPP CDFSPERYQS
LAYNHVLDIH KQHLSPVMTA YFQKPLLLHQ GHMEWLFDSE GNRYLDFFSG IVTVSVGHCH
PKVNAVAQTQ LSRLWHTSSV FFHPPMHEYA EKLSALLPEP LKVIFIVNSG SEANDLAMLM
ARAHTKNTDL ISFRGAYHGC SPYTLGLTNV GNYKTKLPIA MGCQPTMCPD IFRGPWGGSH
CRDSPVQSIR KCSCAPDSCH AKDQYIEQFK DTLNTSVAKS IAGFFAEPIQ GVNGVVQYPK
GFLKEAFQLV RKQGGVCIAD EVQTGFGRLG SHFWGFQTHD VLPDIVTMAK GIGNGFPMAA
VVTTPEIAKS LAQSLLHFNT FGGGPLACAI GSAVLEVIKE EKLQENSQEV GTYMLLKFAQ
LRDEFDIVGD VRGKGLMIGI EMVQDKMSRQ PLPIEEINQI HEDCKNMGLL VGRGGIFSQT
FRIAPPMCVT KPEADFAVEV FHCALSQHME RRAKSHH
//
