ID X6PE03_RETFI Unreviewed; 408 AA.
AC X6PE03;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=alanine--glyoxylate transaminase {ECO:0000256|ARBA:ARBA00013049};
DE EC=2.6.1.44 {ECO:0000256|ARBA:ARBA00013049};
GN ORFNames=RFI_00636 {ECO:0000313|EMBL:ETO36426.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO36426.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO36426.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETO36426.1}.
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DR EMBL; ASPP01000688; ETO36426.1; -; Genomic_DNA.
DR AlphaFoldDB; X6PE03; -.
DR EnsemblProtists; ETO36426; ETO36426; RFI_00636.
DR OMA; GSDRVYH; -.
DR OrthoDB; 1010571at2759; -.
DR Proteomes; UP000023152; Unassembled WGS sequence.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
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; 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:SF24; ALANINE--GLYOXYLATE AMINOTRANSFERASE 1; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152}.
FT DOMAIN 86..347
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 408 AA; 45218 MW; 91468818C1512178 CRC64;
MALLAGDKKK KLLMVPGPIE CDQEVLQMIG QPSESVVHPI FIKSFGDCLR NMRKLFCANE
SCQPFILSGG GALGWDCTVV SLLESKKDKA LVLNTGYFGE NFRDCCRAYD IETDELQFPI
GAAANVSDLE KQLKKKKYKL LTITQVETST GVCNDVRELA DTCRRVSPET LIAVDGVCSF
AAVPFYFSDW NIDIAITASQ KALGAPPGLC VMMLSERTCK YLMSEQRKNA VRSWYCNLQQ
WLPIMQGYEK GQICYFSTPN VNLIKALLVS SQQLLNDGLE RSFARHRHAT LSFREAMRAL
NLSLLVPNDD QAAATVTAVW FPPNINPAEF LKYIDDFGVV VSGGLHRKIK TQYFRVGHMG
ISVNPNRTDL LQTVQAIEYA LAKCKVSNFE KGAGISAFTS AFGTVSKL
//
