ATTY_RHIME
ID ATTY_RHIME Reviewed; 389 AA.
AC Q02636;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Tyrosine aminotransferase;
DE Short=TAT;
DE EC=2.6.1.5;
DE AltName: Full=L-tyrosine:2-oxoglutarate aminotransferase;
GN Name=tatA; OrderedLocusNames=R00307; ORFNames=SMc00387;
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].
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].
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).
CC -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts
CC tyrosine to p-hydroxyphenylpyruvate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 2/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; L05065; AAA26362.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC41744.1; -; Genomic_DNA.
DR PIR; B47094; B47094.
DR RefSeq; NP_384413.1; NC_003047.1.
DR RefSeq; WP_010968491.1; NC_003047.1.
DR AlphaFoldDB; Q02636; -.
DR SMR; Q02636; -.
DR STRING; 266834.SMc00387; -.
DR PRIDE; Q02636; -.
DR EnsemblBacteria; CAC41744; CAC41744; SMc00387.
DR GeneID; 61601787; -.
DR KEGG; sme:SMc00387; -.
DR PATRIC; fig|266834.11.peg.1677; -.
DR eggNOG; COG1448; Bacteria.
DR HOGENOM; CLU_032440_0_1_5; -.
DR OMA; VGACTIV; -.
DR UniPathway; UPA00139; UER00338.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
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 PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Phenylalanine catabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase; Tyrosine catabolism.
FT CHAIN 1..389
FT /note="Tyrosine aminotransferase"
FT /id="PRO_0000123891"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 41937 MW; 45E4DA2DC5A70670 CRC64;
MFDALARQAD DPLLALIGLF RKDERPGKVD LGVGVYRDET GRTPIFRAVK AAEKRLLETQ
DSKAYIGPEG DLVFLDRLWE LVGGDTIERS HVAGVQTPGG SGALRLAADL IARMGGRGIW
LGLPSWPNHA PIFKAAGLDI ATYDFFDIPS QSVIFDNLVS ALEGAASGDA VLLHASCHNP
TGGVLSEAQW MEIAALVAER GLLPLVDLAY QGFGRGLDQD VAGLRHLLGV VPEALVAVSC
SKSFGLYRER AGAIFARTSS TASADRVRSN LAGLARTSYS MPPDHGAAVV RTILDDPELR
RDWTEELETM RLRMTGLRRS LAEGLRTRWQ SLGAVADQEG MFSMLPLSEA EVMRLRTEHG
IYMPASGRIN IAGLKTAEAA EIAGKFTSL
