AAT_RHIME
ID AAT_RHIME Reviewed; 410 AA.
AC P58350;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Aspartate aminotransferase {ECO:0000250|UniProtKB:Q06191};
DE Short=AAT {ECO:0000250|UniProtKB:Q06191};
DE Short=AspAT {ECO:0000250|UniProtKB:Q06191};
DE EC=2.6.1.1 {ECO:0000250|UniProtKB:Q06191};
DE AltName: Full=Putative 2-aminoadipate transaminase {ECO:0000305|PubMed:29769716};
DE EC=2.6.1.39 {ECO:0000305|PubMed:29769716};
DE AltName: Full=Transaminase A {ECO:0000305};
GN Name=aatB; OrderedLocusNames=R03291; ORFNames=SMc04386;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JJ1c10;
RA Watson R.J., Heys R.;
RT "Sinorhizobium meliloti aatB gene region.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION [LARGE SCALE ANALYSIS], AND CATALYTIC ACTIVITY.
RX PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL Nature 557:503-509(2018).
RN [5] {ECO:0007744|PDB:6F35}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, AND SUBUNIT.
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 (By similarity). Genetic
CC evidence shows that this protein is involved in L-lysine catabolism. It
CC may have 2-aminoadipate:2-oxoglutarate aminotransferase activity
CC (PubMed:29769716). {ECO:0000250|UniProtKB:Q06191,
CC ECO:0000269|PubMed:29769716}.
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:0000250|UniProtKB:Q06191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-
CC glutamate; Xref=Rhea:RHEA:12601, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57499, ChEBI:CHEBI:58672; EC=2.6.1.39;
CC Evidence={ECO:0000305|PubMed:29769716};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:30771275};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30771275}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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; AF448466; AAL41013.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC47870.1; -; Genomic_DNA.
DR RefSeq; NP_387397.1; NC_003047.1.
DR RefSeq; WP_010970548.1; NC_003047.1.
DR PDB; 6F35; X-ray; 1.90 A; A/B=1-410.
DR PDBsum; 6F35; -.
DR AlphaFoldDB; P58350; -.
DR SMR; P58350; -.
DR STRING; 266834.SMc04386; -.
DR PRIDE; P58350; -.
DR EnsemblBacteria; CAC47870; CAC47870; SMc04386.
DR GeneID; 61604750; -.
DR KEGG; sme:SMc04386; -.
DR PATRIC; fig|266834.11.peg.4851; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_5; -.
DR OMA; SQGANQY; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047536; F:2-aminoadipate transaminase 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..410
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000123848"
FT BINDING 47
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 135
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 185
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 385
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MOD_RES 249
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:30771275"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:6F35"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6F35"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:6F35"
FT TURN 248..252
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 300..319
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:6F35"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:6F35"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:6F35"
SQ SEQUENCE 410 AA; 44375 MW; DC720126C0C654DB CRC64;
MTINATVKEA GFQPASRISS IGVSEILKIG ARAAAMKREG KPVIILGAGE PDFDTPEHVK
QAASDAIHRG ETKYTALDGT PELKKAIREK FQRENGLAYE LDEITVATGA KQILFNAMMA
SLDPGDEVII PTPYWTSYSD IVHICEGKPV LIACDASSGF RLTAEKLEAA ITPRTRWVLL
NSPSNPSGAA YSAADYRPLL EVLLRHPHVW LLVDDMYEHI VYDGFRFVTP AQLEPGLKNR
TLTVNGVSKA YAMTGWRIGY AGGPRELIKA MAVVQSQATS CPSSISQAAS VAALNGPQDF
LKERTESFQR RRDLVVNGLN AIDGLDCRVP EGAFYTFSGC AGVLGKVTPS GKRIKTDTDF
CAYLLEDAHV AVVPGSAFGL SPFFRISYAT SEAELKEALE RIAAACDRLS
