YBDL_ECOLI
ID YBDL_ECOLI Reviewed; 386 AA.
AC P77806;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Methionine aminotransferase;
DE EC=2.6.1.88;
DE AltName: Full=Methionine-oxo-acid transaminase;
GN Name=ybdL; OrderedLocusNames=b0600, JW0593;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND PYRIDOXAL PHOSPHATE AT LYS-236.
RX PubMed=15280032; DOI=10.1016/j.febslet.2004.06.075;
RA Dolzan M., Johansson K., Roig-Zamboni V., Campanacci V., Tegoni M.,
RA Schneider G., Cambillau C.;
RT "Crystal structure and reactivity of YbdL from Escherichia coli identify a
RT methionine aminotransferase function.";
RL FEBS Lett. 571:141-146(2004).
CC -!- FUNCTION: Shows aminotransferase activity with methionine and histidine
CC as substrates, and to a lesser extent also with phenylalanine.
CC {ECO:0000269|PubMed:15280032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + L-methionine = 4-methylsulfanyl-2-
CC oxobutanoate + an L-alpha-amino acid; Xref=Rhea:RHEA:31763,
CC ChEBI:CHEBI:16723, ChEBI:CHEBI:35179, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59869; EC=2.6.1.88;
CC Evidence={ECO:0000269|PubMed:15280032};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15280032}.
CC -!- INTERACTION:
CC P77806; P69441: adk; NbExp=3; IntAct=EBI-543661, EBI-543592;
CC P77806; P0ABI8: cyoB; NbExp=3; IntAct=EBI-543661, EBI-2932021;
CC P77806; P10443: dnaE; NbExp=3; IntAct=EBI-543661, EBI-549111;
CC P77806; P68646: fixX; NbExp=3; IntAct=EBI-543661, EBI-1113234;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; U82598; AAB40801.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73701.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35230.1; -; Genomic_DNA.
DR PIR; F64793; F64793.
DR RefSeq; NP_415133.1; NC_000913.3.
DR RefSeq; WP_000183907.1; NZ_SSZK01000032.1.
DR PDB; 1U08; X-ray; 2.35 A; A/B=1-386.
DR PDBsum; 1U08; -.
DR AlphaFoldDB; P77806; -.
DR SMR; P77806; -.
DR BioGRID; 4260981; 15.
DR BioGRID; 849596; 9.
DR DIP; DIP-11350N; -.
DR IntAct; P77806; 14.
DR STRING; 511145.b0600; -.
DR PaxDb; P77806; -.
DR PRIDE; P77806; -.
DR EnsemblBacteria; AAC73701; AAC73701; b0600.
DR EnsemblBacteria; BAA35230; BAA35230; BAA35230.
DR GeneID; 945211; -.
DR KEGG; ecj:JW0593; -.
DR KEGG; eco:b0600; -.
DR PATRIC; fig|1411691.4.peg.1668; -.
DR EchoBASE; EB3302; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_0_6; -.
DR InParanoid; P77806; -.
DR OMA; SQGANQY; -.
DR PhylomeDB; P77806; -.
DR BioCyc; EcoCyc:G6329-MON; -.
DR BioCyc; MetaCyc:G6329-MON; -.
DR BRENDA; 2.6.1.88; 2026.
DR EvolutionaryTrace; P77806; -.
DR PRO; PR:P77806; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IBA:GO_Central.
DR GO; GO:0010326; F:methionine-oxo-acid transaminase activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..386
FT /note="Methionine aminotransferase"
FT /id="PRO_0000123925"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:1U08"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1U08"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:1U08"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:1U08"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 291..305
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:1U08"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:1U08"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:1U08"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:1U08"
SQ SEQUENCE 386 AA; 42963 MW; A95A782EA910B13F CRC64;
MTNNPLIPQS KLPQLGTTIF TQMSALAQQH QAINLSQGFP DFDGPRYLQE RLAHHVAQGA
NQYAPMTGVQ ALREAIAQKT ERLYGYQPDA DSDITVTAGA TEALYAAITA LVRNGDEVIC
FDPSYDSYAP AIALSGGIVK RMALQPPHFR VDWQEFAALL SERTRLVILN TPHNPSATVW
QQADFAALWQ AIAGHEIFVI SDEVYEHINF SQQGHASVLA HPQLRERAVA VSSFGKTYHM
TGWKVGYCVA PAPISAEIRK VHQYLTFSVN TPAQLALADM LRAEPEHYLA LPDFYRQKRD
ILVNALNESR LEILPCEGTY FLLVDYSAVS TLDDVEFCQW LTQEHGVAAI PLSVFCADPF
PHKLIRLCFA KKESTLLAAA ERLRQL
