Y4UB_SINFN
ID Y4UB_SINFN Reviewed; 467 AA.
AC Q53196;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Uncharacterized aminotransferase y4uB;
DE EC=2.6.1.-;
GN OrderedLocusNames=NGR_a01380; ORFNames=y4uB;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8796346; DOI=10.1101/gr.6.7.590;
RA Freiberg C., Perret X., Broughton W.J., Rosenthal A.;
RT "Sequencing the 500-kb GC-rich symbiotic replicon of Rhizobium sp. NGR234
RT using dye terminators and a thermostable 'sequenase': a beginning.";
RL Genome Res. 6:590-600(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; Z68203; CAA92403.1; -; Genomic_DNA.
DR EMBL; U00090; AAB91874.1; -; Genomic_DNA.
DR RefSeq; NP_444087.1; NC_000914.2.
DR RefSeq; WP_010875176.1; NC_000914.2.
DR AlphaFoldDB; Q53196; -.
DR SMR; Q53196; -.
DR STRING; 394.NGR_a01380; -.
DR EnsemblBacteria; AAB91874; AAB91874; NGR_a01380.
DR KEGG; rhi:NGR_a01380; -.
DR PATRIC; fig|394.7.peg.124; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_1_5; -.
DR OMA; SEANCYR; -.
DR OrthoDB; 478143at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Plasmid; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..467
FT /note="Uncharacterized aminotransferase y4uB"
FT /id="PRO_0000120539"
FT MOD_RES 290
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 51005 MW; 71A96CEB73F9AFBA CRC64;
MTIDIKDISE KDRNTVLHPF TQLKDFATGK LREPTIVETG KGIRIQDARG NQLIDGFAGL
YCVNVGYGRT EVAEAISRQA YRLAYYHSYA AHTTDELAIL SDRLVKMAPG KMSKVFYGMS
GSDANETQAK LVWYYNNLRG KPTKKKIISR ERGYHGCSVV SGSMTGMSFY HDHMDLPLPQ
ICHTGVPHHY WGANPGETER EFSARRAAEL DEMIETLGPD NVGAFIAEPV LGTGGITPPP
EGYWEAIQAV LKKHDVLLIA DEVITGFGRT GSMFGSQHYG IEPDLITVAK GLTSAYFPLS
ASIVGEKVYK VLEDGADRVG AFSHGYTYSG HPIGAAAANA VLDIVEKEDL PGNAREVGGY
FQAQLKEKFA QLPIVGEVRG VGLMGAIEFV GDRENKKRFD PLLKVGARVS KAARDRGLIA
RAMPHGDILG FAPPLVTTKE EVDEIVAMAE KAVRSVMDEL VRDGQKL