ID A0A1U8ANJ7_NELNU Unreviewed; 469 AA.
AC A0A1U8ANJ7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial {ECO:0000313|RefSeq:XP_010269122.1};
GN Name=LOC104605885 {ECO:0000313|RefSeq:XP_010269122.1};
GN ORFNames=HUJ06_023317 {ECO:0000313|EMBL:DAD21854.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010269122.1};
RN [1] {ECO:0000313|EMBL:DAD21854.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD21854.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010269122.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; DUZY01000001; DAD21854.1; -; Genomic_DNA.
DR RefSeq; XP_010269122.1; XM_010270820.2.
DR STRING; 4432.A0A1U8ANJ7; -.
DR GeneID; 104605885; -.
DR KEGG; nnu:104605885; -.
DR eggNOG; KOG1404; Eukaryota.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009436; P:glyoxylate catabolic process; IBA:GO_Central.
DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; IBA:GO_Central.
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|RefSeq:XP_010269122.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Transferase {ECO:0000313|RefSeq:XP_010269122.1}.
SQ SEQUENCE 469 AA; 51196 MW; 5A00CD83F22D741F CRC64;
MALRRNILKQ SLQTKEKFRH LLLCDFSSIS APKLPPFDYE PKPYKGPSAD EVLEKRKKFL
GPSLFYYYQK PLNIVEGKMQ YLFDDTGRRY LDAFAGIVTV SCGHCHPDVL NAVVEQSKLL
QHATTIYLHH AIADFAEALA SKMPGNLKVV YFVNSGTEAN ELAMLMARLY SGNLGMIALR
NAYHGGSSGT IGLTALNTWK YSIPQGEIHH VINPDPYHGV FGSDASRYAK DVQDHINYGT
SGKVAGFIAE TIQGVGGAVE LAPGYLKLVY DIVRKAGGVC IADEVQTGFG RTGSHYWGFE
TQGVIPDIVT MAKGIGNGLP LGAVVTTPEI ANVMAQKVQF NTFGGNPVCS AGGLAVLRVL
DKEKRQAHCA DVGSHLIERL RALQQKHEII GDVRGRGLMV GIELVTDRKE KMPAKAETAA
LFEKLRELGV LVGKGGLHGN VFRIKPPMCF TKDDADFLVD ALDYSISKL
//
