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Database: UniProt
Entry: I1MK74_SOYBN
LinkDB: I1MK74_SOYBN
Original site: I1MK74_SOYBN 
ID   I1MK74_SOYBN            Unreviewed;       526 AA.
AC   I1MK74;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=GLYMA_16G013900 {ECO:0000313|EMBL:KRH06284.1};
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:KRH06284.1};
RN   [1] {ECO:0000313|EMBL:KRH06284.1, ECO:0000313|EnsemblPlants:KRH06284}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH06284};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH06284.1};
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:KRH06284}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH06284};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH06284.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH06284.1};
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; CM000849; KRH06284.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1MK74; -.
DR   EnsemblPlants; KRH06284; KRH06284; GLYMA_16G013900.
DR   Gramene; KRH06284; KRH06284; GLYMA_16G013900.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000008827; Chromosome 16.
DR   ExpressionAtlas; I1MK74; baseline and differential.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
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:SF29; ALANINE TRANSAMINASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          148..512
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   COILED          405..432
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   526 AA;  58323 MW;  FAE97B867A3382A5 CRC64;
     MRKSAADRFR HLFNRSLILL RHRHHHHPFP SSSSLSPFSR SRFFSSTPFS MASDSPFPVT
     AQNINPKVLK CEYAVRGEVV TLAQNLQKDL QANPGSHPFD ESLGQQPITF FREVLALCDH
     PAILDKSETQ GLFSTDAIQR AWQIVDQIPG RATGAYSHSQ GVKGLRDTIA AGIEERDGFP
     ANPDDIFMTD GASPAVHNMM QLLIRSENDG ILCPIPQYPL YSASIDLHGG FLVPYYLDEA
     TGWGLEIPEL KKQLEAAKSK GINVRALVVI NPGNPTGQVL GEENQRDIVE FCKQEGLVLL
     ADEVYQENVY VPEKKFHSFK KVSRSMGYGE NDITLVSFQS VSKGYHGECG KRGGYMEVTG
     FSAEVREQIY KVASVNLCSN ISGQILASLV MSPPKVGDES YESFNAEKEN ILESLARRAK
     TLEDAFNKLE GVTCNKAEGA MYLFPQIRLS QKAIKAAGDA NTAPDNFYCK RLLNATGVVV
     VPGSGFGQVP GTWHFRCTIL PPEEKIPAIV TRLTEFHEKF MDEFRD
//
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