ID M7B8F2_CHEMY Unreviewed; 473 AA.
AC M7B8F2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=UY3_11069 {ECO:0000313|EMBL:EMP31800.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP31800.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB543353; EMP31800.1; -; Genomic_DNA.
DR AlphaFoldDB; M7B8F2; -.
DR STRING; 8469.M7B8F2; -.
DR eggNOG; KOG1404; Eukaryota.
DR Proteomes; UP000031443; 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; 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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EMP31800.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transferase {ECO:0000313|EMBL:EMP31800.1}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP31800.1"
FT NON_TER 473
FT /evidence="ECO:0000313|EMBL:EMP31800.1"
SQ SEQUENCE 473 AA; 52358 MW; F1515C60685E9B5E CRC64;
SFSMQAKMPP CDFSPGKYES YPYERMLKIR KQNLSPSLVT YYKKPLLLHQ GHMQWLFDYE
GRRYLDLFAG IVTVSVGHCH PKVTAAAQKQ LGHLWHTTNI YMHPSIQEYV EKLTALLPDP
LKVVYLTNSG SEANDLAMFM ARLYTRNFDL ICFRGGYHGG SPYALGLTSI GSYKHGVANG
FGCQTTMLPD VFRGPWGGSH CRDSLVQTIR KCSCSQGCCE ANDQYVEQFK DTLSTCVTKA
IAGFIAEPIQ GVNGAVQYPK RFLKEAFQLV RERGGICIAD EVQTGFGRTG SHFWGFQTHG
VVPDVVTMAK GIGNGFPMAA VVTTPEIANS LAQNLHFNTF GGNPLACVVG SAVLDAIAED
GLQKNSEEVG TYMLLEFAKL RDKFEIIGDV RGKGLMIGIE MVKNKDSRQP LPAEEMNQIW
EDCKDMGVLI GRGGIYSQTF RVKPPMCITK QDAAFAVEVF HAALMRHLER TAA
//
