ID G7JFL4_MEDTR Unreviewed; 373 AA.
AC G7JFL4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011946};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN Name=11438625 {ECO:0000313|EnsemblPlants:AES92497};
GN OrderedLocusNames=MTR_4g130680 {ECO:0000313|EMBL:AES92497.1};
GN ORFNames=MtrunA17_Chr4g0073831 {ECO:0000313|EMBL:RHN64876.1};
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:AES92497.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES92497.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES92497.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES92497,
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:AES92497.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:AES92497.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES92497,
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 [3] {ECO:0000313|EnsemblPlants:AES92497}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES92497};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0007829|PDB:6CZL, ECO:0007829|PDB:6CZM}
RP X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 25-373 IN COMPLEX WITH AMP.
RX PubMed=30072492; DOI=10.1042/BCJ20180289;
RA Ruszkowski M.;
RT "Guarding the gateway to histidine biosynthesis in plants: <i>Medicago
RT truncatula</i> ATP-phosphoribosyltransferase in relaxed and tense states.";
RL Biochem. J. 475:2681-2697(2018).
RN [5] {ECO:0000313|Proteomes:UP000265566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566};
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [6] {ECO:0000313|EMBL:RHN64876.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN64876.1};
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=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:73183; EC=2.4.2.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000915};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC {ECO:0000256|ARBA:ARBA00004667}.
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DR EMBL; CM001220; AES92497.1; -; Genomic_DNA.
DR EMBL; PSQE01000004; RHN64876.1; -; Genomic_DNA.
DR RefSeq; XP_003610300.1; XM_003610252.2.
DR PDB; 6CZL; X-ray; 2.92 A; A/B/C/D/E/F=25-373.
DR PDB; 6CZM; X-ray; 2.88 A; A/B/C/D/E/F=25-373.
DR PDBsum; 6CZL; -.
DR PDBsum; 6CZM; -.
DR STRING; 3880.G7JFL4; -.
DR PaxDb; 3880-AES92497; -.
DR EnsemblPlants; AES92497; AES92497; MTR_4g130680.
DR GeneID; 11438625; -.
DR Gramene; AES92497; AES92497; MTR_4g130680.
DR KEGG; mtr:11438625; -.
DR eggNOG; KOG2831; Eukaryota.
DR HOGENOM; CLU_038115_0_0_1; -.
DR OMA; ITAKKYV; -.
DR OrthoDB; 925at2759; -.
DR BRENDA; 2.4.2.17; 3201.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000002051; Chromosome 4.
DR Proteomes; UP000265566; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR CDD; cd13593; PBP2_HisGL3; 1.
DR Gene3D; 3.30.70.120; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR NCBIfam; TIGR00070; hisG; 1.
DR NCBIfam; TIGR03455; HisG_C-term; 1.
DR PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; GlnB-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6CZL, ECO:0007829|PDB:6CZM};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glycosyltransferase {ECO:0000313|EMBL:AES92497.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Nucleotide-binding {ECO:0007829|PDB:6CZM};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RHN64876.1}.
FT DOMAIN 89..264
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 270..354
FT /note="Histidine biosynthesis HisG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08029"
FT BINDING 69
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
FT BINDING 134
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
FT BINDING 199
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
FT BINDING 212
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
FT BINDING 215
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
FT BINDING 216
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
FT BINDING 217
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
FT BINDING 218
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
FT BINDING 219
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:6CZM"
SQ SEQUENCE 373 AA; 40968 MW; D917D1836BC553FE CRC64;
MLTMMSQIRL PLYCCYASST SISETHHQVL NGNTVSRQEI RLGLPSKGRM SSDTLDLLKD
CQLSVKQVNP RQYVAQIPQI SNLEVWFQRP KDIVRKLLSG DLDLGIVGLD VLTEFGQGNE
DLIVVHEALE YGDCRLSIAI PQYGIFENVN SLEELAKMPQ WTEDKPLRVA TGFTYLGPKF
MKDNGIKHVA FSTADGALEA APAMGIADAI LDLVSSGTTL KENNLKEIEG GTVLESQAAL
VASRRSMIGR KGVLETTHEM LERLEAHLRA MGQFTVVANM RGSSAEEVAE RVLSQPSLAG
LQGPTVSPVF CKRDGKVSAD YYAIVICVPK KALYKSIQQL RAIGGSGVLV SPLTYIFDEE
TPRWRQLLSK LGL
//
