UniProt: I3SQ86

Database: UniProt
Entry: I3SQ86_MEDTR

LinkDB:  I3SQ86_MEDTR 
Original site:  I3SQ86_MEDTR

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (6)   
   InterPro (5)   
   Pfam (1)   
Literature (2)   
   PubMed (2)   
All databases (20)   

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ID   I3SQ86_MEDTR            Unreviewed;       344 AA.
AC   I3SQ86;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=aminodeoxychorismate lyase {ECO:0000256|ARBA:ARBA00035676};
DE            EC=4.1.3.38 {ECO:0000256|ARBA:ARBA00035676};
GN   Name=25487305 {ECO:0000313|EnsemblPlants:KEH38686};
GN   OrderedLocusNames=MTR_2g078730 {ECO:0000313|EMBL:KEH38686.1};
GN   ORFNames=MtrunA17_Chr2g0316981 {ECO:0000313|EMBL:RHN75054.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AFK42428.1};
RN   [1] {ECO:0000313|EMBL:KEH38686.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH38686.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH38686,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AFK42428.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KEH38686.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH38686.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH38686,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [4] {ECO:0000313|EnsemblPlants:KEH38686}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH38686};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [5] {ECO:0000313|EMBL:RHN75054.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN75054.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate;
CC         Xref=Rhea:RHEA:16201, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17836, ChEBI:CHEBI:58406; EC=4.1.3.38;
CC         Evidence={ECO:0000256|ARBA:ARBA00035576};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC       aminobenzoate from chorismate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00035633}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR   EMBL; BT142634; AFK42428.1; -; mRNA.
DR   EMBL; CM001218; KEH38686.1; -; Genomic_DNA.
DR   EMBL; PSQE01000002; RHN75054.1; -; Genomic_DNA.
DR   RefSeq; XP_013464651.1; XM_013609197.1.
DR   AlphaFoldDB; I3SQ86; -.
DR   STRING; 3880.I3SQ86; -.
DR   EnsemblPlants; KEH38686; KEH38686; MTR_2g078730.
DR   GeneID; 25487305; -.
DR   Gramene; KEH38686; KEH38686; MTR_2g078730.
DR   KEGG; mtr:25487305; -.
DR   HOGENOM; CLU_020844_0_0_1; -.
DR   OrthoDB; 1050601at2759; -.
DR   Proteomes; UP000002051; Chromosome 2.
DR   Proteomes; UP000265566; Chromosome 2.
DR   ExpressionAtlas; I3SQ86; differential.
DR   GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047810; F:D-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01559; ADCL_like; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR017824; Aminodeoxychorismate_lyase_IV.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF8; OS01G0238500 PROTEIN; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase {ECO:0000313|EMBL:KEH38686.1};
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RHN75054.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Transferase {ECO:0000313|EMBL:RHN75054.1}.
SQ   SEQUENCE   344 AA;  37863 MW;  EED4FF6B43BBC65C CRC64;
     MGNPPEATAT SEIEIDGDFK VHVFSSSSEL LEKLHQTWSS VEKQPYPAMY SSVYGGIILD
     PAMMVIPIDD HMVHRGHGVF DTAIIFEGHL YELDVHLDRF LRSASKAKIS SPFPRSTLRS
     ILIQLTAASK LKKGTLRYWL SAGPGDFLLS SSGCPTPAFY AVVIDHDFSQ CKEGVKVITS
     SVPMKAPLFA TMKNVNYLPN VLSVLEAEEK GAFGSIWIDE VGYIAEGPNV NVAFITQEKE
     LVMPFFDNIL YGCTAKRLLE LAPKLVDQGV LKSVTTKNMT VDEARGAVEM MYVGSTLPVL
     PIIMWDDQPI GDGKVGELTM LLSDLLWDDM VAGPDTQRIL VPYV
//

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