Y4QG_SINFN
ID Y4QG_SINFN Reviewed; 448 AA.
AC P55628;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Uncharacterized aminotransferase y4qG;
DE EC=2.6.1.-;
GN OrderedLocusNames=NGR_a01910; ORFNames=y4qG;
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 [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 [2]
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; U00090; AAB91831.1; -; Genomic_DNA.
DR RefSeq; NP_444034.1; NC_000914.2.
DR AlphaFoldDB; P55628; -.
DR SMR; P55628; -.
DR STRING; 394.NGR_a01910; -.
DR EnsemblBacteria; AAB91831; AAB91831; NGR_a01910.
DR KEGG; rhi:NGR_a01910; -.
DR PATRIC; fig|394.7.peg.190; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_5; -.
DR OMA; ELDQWKP; -.
DR OrthoDB; 386839at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
DR GO; GO:0047307; F:diaminobutyrate-pyruvate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019491; P:ectoine biosynthetic process; IEA:InterPro.
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; IPR004637; Dat.
DR InterPro; IPR012773; Ectoine_EctB.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43552; PTHR43552; 1.
DR PANTHER; PTHR43552:SF2; PTHR43552:SF2; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00709; dat; 1.
DR TIGRFAMs; TIGR02407; ectoine_ectB; 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..448
FT /note="Uncharacterized aminotransferase y4qG"
FT /id="PRO_0000120538"
FT MOD_RES 297
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 448 AA; 49272 MW; 69982655F3196C5A CRC64;
MWHWHRFQEH EARRSDAIVL LRKIMSNESK SNSLYAFESL ESNVRFYSRS FPVVFEKAAG
AILHDESGRE FIDFLSGSGV LNYGHNDPYF LDEATQYLRS NGIIHGLDMA TPAKREFMEC
FDAIILRPRG LTYKFQFCGP TGANAVEAAL KLARKATGRH SIVSFTNGFH GMSLGALAVT
GNRYYRDAAG FPPAGVAFMP YDGYWGADND TSEYLDKVLA DASSGVDVPA AIILETVQGE
GGINAARKEW LQSIQRICRS HGILLIVDDI QAGCGRAGNF FSFEFAGLSP DVVVLSKSIS
GCGLPLSLLL LKPELDVWRP GEHNGTFRGN NLAFVTGAAA LRKYWTNDAL SARVMETGRI
IAERLRQVAQ TNRARSLSVR GRGMMLGLNC GTGKLAERIV RKAFEEGLVV ERCGAEDQVI
KLLPPLTTDE QTLRRGLDIL HKSVAASI