ID   D8RBH6_SELML            Unreviewed;       481 AA.
AC   D8RBH6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=SELMODRAFT_145611 {ECO:0000313|EMBL:EFJ30498.1},
GN   SELMODRAFT_267931 {ECO:0000313|EMBL:EFJ23041.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ30498.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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; GL377594; EFJ23041.1; -; Genomic_DNA.
DR   EMBL; GL377575; EFJ30498.1; -; Genomic_DNA.
DR   RefSeq; XP_002968244.1; XM_002968198.1.
DR   RefSeq; XP_002976136.1; XM_002976090.1.
DR   AlphaFoldDB; D8RBH6; -.
DR   STRING; 88036.D8RBH6; -.
DR   EnsemblPlants; EFJ23041; EFJ23041; SELMODRAFT_267931.
DR   EnsemblPlants; EFJ30498; EFJ30498; SELMODRAFT_145611.
DR   GeneID; 9631419; -.
DR   GeneID; 9645831; -.
DR   Gramene; EFJ23041; EFJ23041; SELMODRAFT_267931.
DR   Gramene; EFJ30498; EFJ30498; SELMODRAFT_145611.
DR   KEGG; smo:SELMODRAFT_145611; -.
DR   KEGG; smo:SELMODRAFT_267931; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   InParanoid; D8RBH6; -.
DR   OMA; IGDPNLF; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
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:UP000001514};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          82..447
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   481 AA;  53378 MW;  7FEAFA7E54123592 CRC64;
     MASKVLDPDN INENVKKCVY AVRGELYLRA SELQKEGKKI IFTNVGNPHA LGQKPLTFPR
     QVMALCQAPF LMDDPNVGLL FPPDAVARAK HYLSMTSGGV GAYSDSRGLP GVRQEVAEFI
     QKRDGYPSDP EHIFLTDGAS KGVMMMLNAL IRNEKDGVLV PIPQYPLYSA SIALYGGILI
     PYYLNEESNW SLDFSDVRNQ VVIARNKKIV PRALVFINPG NPTGQCLSVT NLQDLIKFCY
     KERLLLMADE VYQVNVYQDE RPFVSAKKVL MDMGAPYSNT VELVSFHSVS KGFLGECGQR
     GGYFEMTNIH PQTVEELYKV ASISLSPNVV GQIMMGLMVT PPRPFDISYP QYQAESKAII
     ESMRRRAHIM TDGFNKCEDV VCNFTEGAMY SFPRIKLSKA AMDAAAQAGK AADVFYCLKL
     LEATGISTVP GSGFGQKEGT LHLRTTILPL EQDMPGIMAK FQKFHADFMA QYSDYSVSSR
     L
//