AATC_RHIME
ID AATC_RHIME Reviewed; 405 AA.
AC O87320;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative aminotransferase AatC;
DE EC=2.6.1.-;
GN Name=aatC; OrderedLocusNames=R01723; ORFNames=SMc00294;
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 [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 [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-234.
RC STRAIN=1021;
RX PubMed=9734305; DOI=10.1139/w98-033;
RA Willis L.B., Walker G.C.;
RT "The phbC (poly-beta-hydroxybutyrate synthase) gene of Rhizobium
RT (Sinorhizobium) meliloti and characterization of phbC mutants.";
RL Can. J. Microbiol. 44:554-564(1998).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC61900.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL591688; CAC46302.1; -; Genomic_DNA.
DR EMBL; AF031938; AAC61900.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_385829.1; NC_003047.1.
DR RefSeq; WP_010969423.1; NC_003047.1.
DR AlphaFoldDB; O87320; -.
DR SMR; O87320; -.
DR STRING; 266834.SMc00294; -.
DR EnsemblBacteria; CAC46302; CAC46302; SMc00294.
DR GeneID; 61603196; -.
DR KEGG; sme:SMc00294; -.
DR PATRIC; fig|266834.11.peg.3160; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_5; -.
DR OMA; YPHMPTG; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
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; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..405
FT /note="Putative aminotransferase AatC"
FT /id="PRO_0000123923"
FT MOD_RES 238
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 43
FT /note="P -> R (in Ref. 3; AAC61900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 44576 MW; D4A1E708A5F2D473 CRC64;
MEEFHKVRRL PPYVFEQVNR LKASARAAGA DIIDLGMGNP DLPTPQSIVD KLCEVVQDPR
THRYSSSKGI PGLRRAQAAY YARRFGVKLN PETQVVATLG SKEGFANMAQ AITAPGDVVL
CPNPTYPIHA FGFLMAGGVI RSISVEPDES FFPPLERAVR HSIPKPLALI LNYPSNPTAQ
VATLDFYKDV IAFAKKHDII VLSDLAYSEI YFDDAPPPSV LEVPGATDVT VEFTSMSKTF
SMPGWRMGFA VGNERLIAAL TRVKSYLDYG AFTPIQVAAT QALNGDGSDI AEVRAIYKRR
RDVMVESFGK AGFEVPPPPA TMFAWAKIPE KFRHLGSLEF SKLLVEKADV AVAPGIGFGE
QGDDYVRLAL VENEHRIRQA ARNIKRFLSS ADETMHNVIS LNAHR