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Database: UniProt/TrEMBL
Entry: I1JC65_SOYBN
LinkDB: I1JC65_SOYBN
Original site: I1JC65_SOYBN 
ID   I1JC65_SOYBN            Unreviewed;       481 AA.
AC   I1JC65;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=100787173 {ECO:0000313|EnsemblPlants:KRH69622};
GN   ORFNames=GLYMA_02G038100 {ECO:0000313|EMBL:KRH69624.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH69624.1};
RN   [1] {ECO:0000313|EMBL:KRH69624.1, ECO:0000313|EnsemblPlants:KRH69622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH69622};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH69624.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH69622}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH69622};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH69624.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH69624.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00025708}.
CC   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC       {ECO:0000256|ARBA:ARBA00025709}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000256|ARBA:ARBA00025785}.
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DR   EMBL; CM000835; KRH69622.1; -; Genomic_DNA.
DR   EMBL; CM000835; KRH69623.1; -; Genomic_DNA.
DR   EMBL; CM000835; KRH69624.1; -; Genomic_DNA.
DR   RefSeq; XP_003519649.1; XM_003519601.3.
DR   RefSeq; XP_014620255.1; XM_014764769.1.
DR   AlphaFoldDB; I1JC65; -.
DR   SMR; I1JC65; -.
DR   STRING; 3847.I1JC65; -.
DR   PaxDb; 3847-GLYMA02G04320-6; -.
DR   EnsemblPlants; KRH69622; KRH69622; GLYMA_02G038100.
DR   EnsemblPlants; KRH69623; KRH69623; GLYMA_02G038100.
DR   EnsemblPlants; KRH69624; KRH69624; GLYMA_02G038100.
DR   GeneID; 100787173; -.
DR   Gramene; KRH69622; KRH69622; GLYMA_02G038100.
DR   Gramene; KRH69623; KRH69623; GLYMA_02G038100.
DR   Gramene; KRH69624; KRH69624; GLYMA_02G038100.
DR   KEGG; gmx:100787173; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   InParanoid; I1JC65; -.
DR   OMA; IGDPNLF; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000008827; Chromosome 2.
DR   ExpressionAtlas; I1JC65; baseline and differential.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
DR   GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009853; P:photorespiration; IBA:GO_Central.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 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; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF373; ALANINE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          84..447
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   481 AA;  53489 MW;  BE43E58F066DA4B0 CRC64;
     MPPKPLDYGS INENVKKSQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA LGQKPLSFPR
     QVVALCQAPF LLDDPNVGLL FPADAIARAK HYLSLTSGGL GAYSDSRGLP GVRKEVAEFI
     LRRDGYPTDP ELIYLTDGAS KGVMQILNTI IRGQDDGILV PVPQYPLYSA TIALLGGTLV
     PYYLEETANW GLDVNELRQS VEQARFKGIT VKAMVIINPG NPTGQCLSEA NLREVLQFCY
     QENLALLGDE VYQTNIYQDE RPFISSRKVL MELGPPISKE VQLISFHSVS KGYYGECGQR
     GGYFEMTNIP PETVDEIYKV ASISLSPNVP AQIFMGVMLN PPQPGDISYD KFVRESTGIL
     ESLRRRARIM TDGFNSCRNV VCNFTEGAMY SFPQIRLPPR ALEAAKQAGK VPDVYYCLKL
     LEATGISTVP GSGFGQKEGV FHLRTTILPA EEDMPDIMDS FKKFNDEFME QYEDDRGYSR
     L
//
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