GenomeNet

Database: UniProt/TrEMBL
Entry: A9TEP5_PHYPA
LinkDB: A9TEP5_PHYPA
Original site: A9TEP5_PHYPA 
ID   A9TEP5_PHYPA            Unreviewed;       480 AA.
AC   A9TEP5;
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_029419 {ECO:0000313|EMBL:PNR27267.1};
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:PNR27267.1};
RN   [1] {ECO:0000313|EMBL:PNR27267.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c25_700V3.1,
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:PNR27267.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c25_700V3.1,
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:Pp3c25_700V3.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABEU02000025; PNR27267.1; -; Genomic_DNA.
DR   RefSeq; XP_001777071.1; XM_001777019.1.
DR   AlphaFoldDB; A9TEP5; -.
DR   STRING; 3218.A9TEP5; -.
DR   PaxDb; 3218-PP1S215_28V6-1; -.
DR   EnsemblPlants; Pp3c25_700V3.1; Pp3c25_700V3.1; Pp3c25_700.
DR   EnsemblPlants; Pp3c25_700V3.2; Pp3c25_700V3.2; Pp3c25_700.
DR   Gramene; Pp3c25_700V3.1; Pp3c25_700V3.1; Pp3c25_700.
DR   Gramene; Pp3c25_700V3.2; Pp3c25_700V3.2; Pp3c25_700.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   InParanoid; A9TEP5; -.
DR   OMA; QVFNKAP; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000006727; Chromosome 25.
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          83..448
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   480 AA;  52660 MW;  F2ABF0FCC2C29A7B CRC64;
     MASGKVMDPD NLNENVKKTV YAVRGELYLR ASELQKEGKK IIFTNVGNPH ALGQKPLTFP
     RQVMALCQAP FLMDDPHVGL LFPADAIAKA KHYLAMTSGG VGAYSDSRGL PGVRQEVANF
     ILQRDGYPSD PENIFLTDGA SKGVAQVLNA LIRDEKDGVL VPIPQYPLYS ATIQLLGGTL
     VPYYLAEEDN WGLNTNDLRK SVTEARRKGI CVRGLVFINP GNPTGQCLTE KNLRELIEFC
     IKEKIVLMAD EVYQQNVYQD ERPFISARKV LMGMGPPVSE ALELVSFHTV SKGFLGECGQ
     RGGYFEMTNI HPKTVDELYK VSSIALSPNV TGQIMMGLMV SPPKPGDISY PLYKAESEAI
     SLSLRKRAHI MTDGFNACEN IVCNFTEGAM YSFPQVKLPQ AAIAAAKKAG KAPDVFYCLR
     LLEATGISTV PGSGFGQKEG TFHVRTTILP SERDMPGIME SFKKFNADFM AQHSDTKSKL
//
DBGET integrated database retrieval system