ID A9TW32_PHYPA Unreviewed; 480 AA.
AC A9TW32;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=PHYPA_020573 {ECO:0000313|EMBL:PNR37464.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR37464.1};
RN [1] {ECO:0000313|EMBL:PNR37464.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c16_6730V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR37464.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c16_6730V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c16_6730V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
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; ABEU02000016; PNR37464.1; -; Genomic_DNA.
DR RefSeq; XP_001782822.1; XM_001782770.1.
DR AlphaFoldDB; A9TW32; -.
DR STRING; 3218.A9TW32; -.
DR PaxDb; 3218-PP1S341_73V6-2; -.
DR EnsemblPlants; Pp3c16_6730V3.1; Pp3c16_6730V3.1; Pp3c16_6730.
DR EnsemblPlants; Pp3c16_6730V3.2; Pp3c16_6730V3.2; Pp3c16_6730.
DR EnsemblPlants; Pp3c16_6730V3.5; Pp3c16_6730V3.5; Pp3c16_6730.
DR Gramene; Pp3c16_6730V3.1; Pp3c16_6730V3.1; Pp3c16_6730.
DR Gramene; Pp3c16_6730V3.2; Pp3c16_6730V3.2; Pp3c16_6730.
DR Gramene; Pp3c16_6730V3.5; Pp3c16_6730V3.5; Pp3c16_6730.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_0_1; -.
DR InParanoid; A9TW32; -.
DR OMA; IGDPNLF; -.
DR OrthoDB; 5472891at2759; -.
DR UniPathway; UPA00322; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000006727; Chromosome 16.
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:UP000006727};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 84..452
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 480 AA; 52723 MW; B3B9B1B2A7223A96 CRC64;
MASGKVMDPE NLNENVKKTV YAVRGELYLR ASELQKEGKK IIFTNVGNPH ALGQKPLTFP
RQVMALCQAP FLMDDPHVGL LFPADAIAKA KHYLSMTSGG VGAYSDSRGL PGVRQEVANF
ILQRDGYPSD PENIFLTDGA SKGVAQVLNA LIRDEKDGVL VPIPQYPLYS ATIQLLGGTL
VPYYLTEEEN WGMSINELRR SVTEARRKGI CVRGLVFINP GNPTGQCLTE KNLGELIEFC
IQERIVLMAD EVYQQNVYQD ERPFISARKV LMGMGPPASE ALELVSFHTV SKGFLGECGQ
RGGYFEMTNF HPKTVDELYK VSSIALSPNV SGQIMMGLMV NPPKPGDISY PQYEAESKAI
SLSLRKRAHI MTDGFNACEN VVCNFTEGAM YSFPQVKLPQ AAVAAAKKAG KAPDVFYCLR
LLEATGISTV PGSGFGQKEG TFHVRTTILP SEKDMPGIME SFKKFNQDFM AQYADAKSKL
//
