AAPAT_RHIME
ID AAPAT_RHIME Reviewed; 400 AA.
AC Q02635;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Aspartate/prephenate aminotransferase {ECO:0000305};
DE Short=AspAT / PAT {ECO:0000305};
DE EC=2.6.1.1 {ECO:0000269|PubMed:24302739, ECO:0000269|PubMed:8096210};
DE EC=2.6.1.79 {ECO:0000269|PubMed:24302739};
DE AltName: Full=Transaminase A;
GN Name=aatA {ECO:0000303|PubMed:8096210}; OrderedLocusNames=R02325;
GN ORFNames=SMc01578;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=JJ1c10;
RX PubMed=2019560; DOI=10.1128/jb.173.9.2879-2887.1991;
RA Rastogi V.K., Watson R.J.;
RT "Aspartate aminotransferase activity is required for aspartate catabolism
RT and symbiotic nitrogen fixation in Rhizobium meliloti.";
RL J. Bacteriol. 173:2879-2887(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=JJ1c10;
RX PubMed=8096210; DOI=10.1128/jb.175.7.1919-1928.1993;
RA Watson R.J., Rastogi V.K.;
RT "Cloning and nucleotide sequencing of Rhizobium meliloti aminotransferase
RT genes: an aspartate aminotransferase required for symbiotic nitrogen
RT fixation is atypical.";
RL J. Bacteriol. 175:1919-1928(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=RCR2011;
RX PubMed=24302739; DOI=10.1074/jbc.m113.486480;
RA Graindorge M., Giustini C., Kraut A., Moyet L., Curien G., Matringe M.;
RT "Three different classes of aminotransferases evolved prephenate
RT aminotransferase functionality in arogenate-competent microorganisms.";
RL J. Biol. Chem. 289:3198-3208(2014).
RN [6] {ECO:0007744|PDB:6F77}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS), COFACTOR, SUBUNIT, AND MUTAGENESIS
RP OF LYS-12.
RX PubMed=30771275; DOI=10.1111/febs.14789;
RA Giustini C., Graindorge M., Cobessi D., Crouzy S., Robin A., Curien G.,
RA Matringe M.;
RT "Tyrosine metabolism: identification of a key residue in the acquisition of
RT prephenate aminotransferase activity by 1beta aspartate aminotransferase.";
RL FEBS J. 286:2118-2134(2019).
CC -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC oxoglutarate to glutamate and oxaloacetate (PubMed:8096210,
CC PubMed:24302739). Can also transaminate prephenate in the presence of
CC glutamate (PubMed:24302739). Required for symbiotic nitrogen fixation
CC (PubMed:2019560). {ECO:0000269|PubMed:2019560,
CC ECO:0000269|PubMed:24302739, ECO:0000269|PubMed:8096210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000269|PubMed:24302739, ECO:0000269|PubMed:8096210};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-arogenate = L-glutamate + prephenate;
CC Xref=Rhea:RHEA:22880, ChEBI:CHEBI:16810, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58180; EC=2.6.1.79;
CC Evidence={ECO:0000269|PubMed:24302739};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:30771275};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for oxaloacetate {ECO:0000269|PubMed:24302739};
CC KM=100 uM for prephenate {ECO:0000269|PubMed:24302739};
CC Note=kcat is 205 sec(-1) with oxaloacetate as substrate. kcat is 43
CC sec(-1) with prephenate as substrate. {ECO:0000269|PubMed:24302739};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30771275}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to grow on aspartate but can
CC grow on other carbon and nitrogen sources. Mutant is unable to fix
CC nitrogen within nodules formed on alfalfa.
CC {ECO:0000269|PubMed:2019560}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; L05064; AAA26245.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC46904.1; -; Genomic_DNA.
DR PIR; A47094; A47094.
DR RefSeq; NP_386431.1; NC_003047.1.
DR RefSeq; WP_010969860.1; NC_003047.1.
DR PDB; 6F77; X-ray; 1.79 A; A/B/C/D/E/F=1-400.
DR PDBsum; 6F77; -.
DR AlphaFoldDB; Q02635; -.
DR SMR; Q02635; -.
DR STRING; 266834.SMc01578; -.
DR EnsemblBacteria; CAC46904; CAC46904; SMc01578.
DR GeneID; 61603789; -.
DR KEGG; sme:SMc01578; -.
DR PATRIC; fig|266834.11.peg.3805; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_5; -.
DR OMA; APYWTTY; -.
DR BRENDA; 2.6.1.1; 5347.
DR BRENDA; 2.6.1.78; 5347.
DR BRENDA; 2.6.1.79; 5347.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033854; F:glutamate-prephenate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..400
FT /note="Aspartate/prephenate aminotransferase"
FT /id="PRO_0000123847"
FT BINDING 39
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 125
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 175
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 375
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT SITE 12
FT /note="Important for prephenate aminotransferase activity"
FT /evidence="ECO:0000269|PubMed:30771275"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MUTAGEN 12
FT /note="K->G: 7-fold increase in Km for prephenate. Weakly
FT affects Km for oxaloacetate."
FT /evidence="ECO:0000269|PubMed:30771275"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 71..85
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6F77"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:6F77"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:6F77"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:6F77"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:6F77"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:6F77"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6F77"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:6F77"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:6F77"
FT TURN 238..242
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6F77"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 289..309
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 347..358
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:6F77"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:6F77"
FT HELIX 382..398
FT /evidence="ECO:0007829|PDB:6F77"
SQ SEQUENCE 400 AA; 43583 MW; 34668FAE196660D6 CRC64;
MAFLADALSR VKPSATIAVS QKARELKAKG RDVIGLGAGE PDFDTPDNIK KAAIDAIDRG
ETKYTPVSGI PELREAIAKK FKRENNLDYT AAQTIVGTGG KQILFNAFMA TLNPGDEVVI
PAPYWVSYPE MVALCGGTPV FVPTRQENNF KLKAEDLDRA ITPKTKWFVF NSPSNPSGAA
YSHEELKALT DVLMKHPHVW VLTDDMYEHL TYGDFRFATP VEVEPGLYER TLTMNGVSKA
YAMTGWRIGY AAGPLHLIKA MDMIQGQQTS GAASIAQWAA VEALNGPQDF IGRNKEIFQG
RRDLVVSMLN QAKGISCPTP EGAFYVYPSC AGLIGKTAPS GKVIETDEDF VSELLETEGV
AVVHGSAFGL GPNFRISYAT SEALLEEACR RIQRFCAACR
