RHBA_RHIME
ID RHBA_RHIME Reviewed; 470 AA.
AC Q9Z3R2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase;
DE EC=2.6.1.76;
DE AltName: Full=Diaminobutyrate transaminase;
DE AltName: Full=L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase;
DE Short=DABA aminotransferase;
DE Short=DABA-AT;
DE AltName: Full=L-diaminobutyric acid transaminase;
GN Name=rhbA; Synonyms=rhsA; OrderedLocusNames=RA1258; ORFNames=SMa2400;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RCR2011 / SU47;
RX PubMed=11274118; DOI=10.1128/jb.183.8.2576-2585.2001;
RA Lynch D., O'Brien J., Welch T., Clarke P., Cuiv P.O., Crosa J.H.,
RA O'Connell M.;
RT "Genetic organization of the region encoding regulation, biosynthesis, and
RT transport of rhizobactin 1021, a siderophore produced by Sinorhizobium
RT meliloti.";
RL J. Bacteriol. 183:2576-2585(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [3]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-2,4-diaminobutanoate = L-aspartate 4-
CC semialdehyde + L-glutamate; Xref=Rhea:RHEA:11160, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58761, ChEBI:CHEBI:537519;
CC EC=2.6.1.76;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Siderophore biosynthesis; rhizobactin biosynthesis.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF110737; AAD09412.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65916.1; -; Genomic_DNA.
DR PIR; B95419; B95419.
DR PIR; T46814; T46814.
DR RefSeq; NP_436504.1; NC_003037.1.
DR RefSeq; WP_010968201.1; NC_003037.1.
DR AlphaFoldDB; Q9Z3R2; -.
DR SMR; Q9Z3R2; -.
DR EnsemblBacteria; AAK65916; AAK65916; SMa2400.
DR GeneID; 61599987; -.
DR KEGG; sme:SMa2400; -.
DR PATRIC; fig|266834.11.peg.1311; -.
DR HOGENOM; CLU_016922_10_0_5; -.
DR OMA; AHIGTFR; -.
DR BioCyc; MetaCyc:MON-15538; -.
DR UniPathway; UPA00020; -.
DR Proteomes; UP000001976; Plasmid pSymA.
DR GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019289; P:rhizobactin 1021 biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43552; PTHR43552; 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 PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Plasmid; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..470
FT /note="Diaminobutyrate--2-oxoglutarate aminotransferase"
FT /id="PRO_0000120516"
FT MOD_RES 304
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 50148 MW; 0377B3B8B9A09049 CRC64;
MPADLAARTS SKIFNGVDLM DASARADNAF YLDRQERRES NARSYPRRFP VALKSASGCI
VTDVDGRSYL DCLAGAGTLA LGHNHPEVIE TLQQVLGSGL PLHTLDLTTP VKDRFVSDIF
GTLPAGLRDE AKIQFCSPSG TDAVEAAIKL AKTATGRTDL VSFRGAYHGM SQGSLSLMGS
LGPKASVGQL VPGAHFFPYP YAYRCPFGRG GNETATLAAE YFERALRDPE GGINRPAAVI
LEAVQGEGGV IPAPVEWLRA VRRVTRDLGI PLIVDEVQSG VGRTGSFYAF QKAGIIPDVV
VLSKAIGGGL PLAVVIYRED LDLWKPGAHA GTFRGNQLAM AAGSKTLEII ERERLVERAA
IAGRRLRANL ERIAAQTPYI GEVRGEGLML GVEVVDPEGL PDALGHPPHG QEIARMIQHE
MFRAGIILET GGRFGSVLRL LPPLVISDAE IDQVSGALAA AFERLGRKAA
