ALA2_HORVU
ID ALA2_HORVU Reviewed; 482 AA.
AC P52894;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Alanine aminotransferase 2;
DE Short=ALAAT-2;
DE EC=2.6.1.2;
DE AltName: Full=Glutamate pyruvate transaminase 2;
DE Short=GPT;
DE AltName: Full=Glutamic--alanine transaminase 2;
DE AltName: Full=Glutamic--pyruvic transaminase 2;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Himalaya; TISSUE=Root;
RX PubMed=8123785; DOI=10.1007/bf00024110;
RA Muench D.G., Good A.G.;
RT "Hypoxically inducible barley alanine aminotransferase: cDNA cloning and
RT expression analysis.";
RL Plant Mol. Biol. 24:417-427(1994).
CC -!- FUNCTION: Transfer of C3 units between the cytosol of mesophyll and
CC bundle sheath cells to maintain a nitrogen-carbon balance in the C4-
CC dicarboxylic pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC pathway; pyruvate from L-alanine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. Alanine aminotransferase subfamily.
CC {ECO:0000305}.
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DR EMBL; Z26322; CAA81231.1; -; mRNA.
DR PIR; S42535; S42535.
DR PDB; 3TCM; X-ray; 2.71 A; A/B=1-482.
DR PDBsum; 3TCM; -.
DR AlphaFoldDB; P52894; -.
DR SMR; P52894; -.
DR PRIDE; P52894; -.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0015010.1; HORVU.MOREX.r2.1HG0015010.1; HORVU.MOREX.r2.1HG0015010.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0015010.1.mrna1; HORVU.MOREX.r2.1HG0015010.1.mrna1; HORVU.MOREX.r2.1HG0015010.1.
DR Gramene; HORVU.MOREX.r2.1HG0015010.1; HORVU.MOREX.r2.1HG0015010.1; HORVU.MOREX.r2.1HG0015010.
DR Gramene; HORVU.MOREX.r2.1HG0015010.1.mrna1; HORVU.MOREX.r2.1HG0015010.1.mrna1; HORVU.MOREX.r2.1HG0015010.1.
DR BRENDA; 2.6.1.2; 2687.
DR SABIO-RK; P52894; -.
DR UniPathway; UPA00322; -.
DR UniPathway; UPA00528; UER00586.
DR ExpressionAtlas; P52894; baseline and differential.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11751; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..482
FT /note="Alanine aminotransferase 2"
FT /id="PRO_0000123939"
FT MOD_RES 299
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3TCM"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:3TCM"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:3TCM"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:3TCM"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 337..347
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 356..383
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 407..416
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 420..432
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:3TCM"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:3TCM"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:3TCM"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:3TCM"
FT HELIX 462..480
FT /evidence="ECO:0007829|PDB:3TCM"
SQ SEQUENCE 482 AA; 52877 MW; E84176F7DFB6B2FC CRC64;
MAATVAVDNL NPKVLKCEYA VRGEIVIHAQ RLQEQLKTQP GSLPFDEILY CNIGNPQSLG
QQPVTFFREV LALCDHPDLL QREEIKTLFS ADSISRAKQI LAMIPGRATG AYSHSQGIKG
LRDAIASGIA SRDGFPANAD DIFLTDGASP GVHLMMQLLI RNEKDGILVP IPQYPLYSAS
IALHGGALVP YYLNESTGWG LETSDVKKQL EDARSRGINV RALVVINPGN PTGQVLAEEN
QYDIVKFCKN EGLVLLADEV YQENIYVDNK KFHSFKKIVR SLGYGEEDLP LVSYQSVSKG
YYGECGKRGG YFEITGFSAP VREQIYKIAS VNLCSNITGQ ILASLVMNPP KASDESYASY
KAEKDGILAS LARRAKALEH AFNKLEGITC NEAEGAMYVF PQICLPQKAI EAAKAANKAP
DAFYALRLLE STGIVVVPGS GFGQVPGTWH FRCTILPQED KIPAVISRFT VFHEAFMSEY
RD
