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   27-MAR-2024, entry version 128.
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; Pseudomonadota; 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   KEGG; rhi:NGR_a01380; -.
DR   PATRIC; fig|394.7.peg.124; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_1_5; -.
DR   OrthoDB; 9801834at2; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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
//