RHBB_RHIME
ID RHBB_RHIME Reviewed; 495 AA.
AC Q9Z3R1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=L-2,4-diaminobutyrate decarboxylase;
DE Short=DABA decarboxylase;
DE Short=DABA-DC;
DE EC=4.1.1.86;
GN Name=rhbB; Synonyms=rhsB; OrderedLocusNames=RA1259; ORFNames=SMa2402;
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=H(+) + L-2,4-diaminobutanoate = CO2 + propane-1,3-diamine;
CC Xref=Rhea:RHEA:15689, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57484, ChEBI:CHEBI:58761; EC=4.1.1.86;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Siderophore biosynthesis; rhizobactin biosynthesis.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AF110737; AAD09413.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65917.1; -; Genomic_DNA.
DR PIR; C95419; C95419.
DR PIR; T46815; T46815.
DR RefSeq; NP_436505.1; NC_003037.1.
DR RefSeq; WP_010968202.1; NC_003037.1.
DR AlphaFoldDB; Q9Z3R1; -.
DR SMR; Q9Z3R1; -.
DR EnsemblBacteria; AAK65917; AAK65917; SMa2402.
DR GeneID; 61599988; -.
DR KEGG; sme:SMa2402; -.
DR PATRIC; fig|266834.11.peg.1312; -.
DR HOGENOM; CLU_011856_0_4_5; -.
DR OMA; NPGFNWS; -.
DR BioCyc; MetaCyc:MON-15539; -.
DR UniPathway; UPA00020; -.
DR Proteomes; UP000001976; Plasmid pSymA.
DR GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0019289; P:rhizobactin 1021 biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Plasmid; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..495
FT /note="L-2,4-diaminobutyrate decarboxylase"
FT /id="PRO_0000147005"
FT MOD_RES 312
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 52464 MW; 69C2C1A0EF40D160 CRC64;
MNINVAAFRT PPTKQTDHAD QILGTDSESR RVFRNAMLQA IDMVVDQTAA ASSLYSGTSF
QGLRGLIDDL DPLPEVGTGI AAALAEIGRP ALEHAMVVGH PAAMAHLHCP VAVPALAAEV
LISATNQSLD SWDQSPFATL VEERVLACLT QLAELPASAS GNFTSGGTQS NMTALYLAAV
RCGPDARKAG VVLTSAHAHF SIRKSAAILG FAEDAVIAIA ADADGRMSVP ALKAELLRVA
GEGRIPVAVV ATAGTTDLGA IDPLVEIADL AAAQNVWMHV DAAYGGGLLF SRHRSRLEGL
EHAHSITLDF HKMLFQPISC GVLLLRDRAD FAPLASKADY LNPEDAVFAD APNLVERSMQ
TTRRADALKI LMTMRAIGRD GLDALICQTL QNTHAAAEAV KTREYLSLAG PPSLSTVLFR
YVSARGPKFA DAITLKTRAA LFNAGIAALA TTVLDGRVHF KLTLLNPRST PDVVHRILDA
IGETARELET HHARP
