ID M3ZNH0_XIPMA Unreviewed; 391 AA.
AC M3ZNH0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Alanine--glyoxylate aminotransferase {ECO:0000256|ARBA:ARBA00019220, ECO:0000256|PIRNR:PIRNR000524};
DE Short=AGT {ECO:0000256|PIRNR:PIRNR000524};
DE Short=SPT {ECO:0000256|PIRNR:PIRNR000524};
DE EC=2.6.1.44 {ECO:0000256|ARBA:ARBA00013049, ECO:0000256|PIRNR:PIRNR000524};
DE EC=2.6.1.51 {ECO:0000256|ARBA:ARBA00013027, ECO:0000256|PIRNR:PIRNR000524};
DE AltName: Full=Serine--pyruvate aminotransferase {ECO:0000256|PIRNR:PIRNR000524};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000003763.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000003763.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000003763.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine + pyruvate = 3-hydroxypyruvate + L-alanine;
CC Xref=Rhea:RHEA:22852, ChEBI:CHEBI:15361, ChEBI:CHEBI:17180,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57972; EC=2.6.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00033634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853;
CC Evidence={ECO:0000256|ARBA:ARBA00033634};
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR000524, ECO:0000256|PIRSR:PIRSR000524-50,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000524}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|PIRNR:PIRNR000524, ECO:0000256|RuleBase:RU004075}.
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DR RefSeq; XP_005811406.1; XM_005811349.1.
DR AlphaFoldDB; M3ZNH0; -.
DR STRING; 8083.ENSXMAP00000003763; -.
DR Ensembl; ENSXMAT00000003768.2; ENSXMAP00000003763.1; ENSXMAG00000003741.2.
DR GeneID; 102227198; -.
DR KEGG; xma:102227198; -.
DR CTD; 436603; -.
DR eggNOG; KOG2862; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_027686_0_0_1; -.
DR InParanoid; M3ZNH0; -.
DR OMA; GSDRVYH; -.
DR OrthoDB; 1010571at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR CDD; cd06451; AGAT_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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF22; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR000524};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT DOMAIN 22..361
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 391 AA; 42722 MW; 8C555C72AE7CEB85 CRC64;
MSPVSMPPPQ CLKKRMVVPH RYMFGPGPSN VPRRILEAGA KPVIGHMHPE TFEIMSDIKS
GIQYLFQTQN RTTFAVSGTG HTAMECAIFN TVESGESVLV AVNGIWGERA ADMGERVGAK
VKTIVAPPGG YLTNAEIEKA LSEHRPVLFF LAHGESSTGV LHPLDGIGDL CHKYSCLFLV
DSVASIGGTP LYMDQQGIDI LYTGSQKVLN APPGTAPISF SERACQKVFS RTTKPVSFFL
DLSWLSNYWG CDDKPARIYH HTVPVTALYS LRESLAVLAD EGLEKSWDRH QKVAEYFHAG
LESMGLKLFV KEKHARLPTV TTIVAPHGYD WKEITTYIMK THSLEISGGL GTSVGLVLRV
GLMGCNSSKA NADMVLAALK DALKHCHRSK V
//
