SBNH_STAA8
ID SBNH_STAA8 Reviewed; 400 AA.
AC Q2G1M6; Q6X7U0;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate decarboxylase {ECO:0000305};
DE EC=4.1.1.117 {ECO:0000269|PubMed:19775248};
DE AltName: Full=Staphyloferrin B biosynthesis protein SbnH {ECO:0000305};
GN Name=sbnH {ECO:0000303|PubMed:14688077};
GN OrderedLocusNames=SAOUHSC_00082 {ECO:0000312|EMBL:ABD29265.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=14688077; DOI=10.1128/iai.72.1.29-37.2004;
RA Dale S.E., Doherty-Kirby A., Lajoie G., Heinrichs D.E.;
RT "Role of siderophore biosynthesis in virulence of Staphylococcus aureus:
RT identification and characterization of genes involved in production of a
RT siderophore.";
RL Infect. Immun. 72:29-37(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND SUBUNIT.
RX PubMed=19775248; DOI=10.1111/j.1365-2958.2009.06880.x;
RA Cheung J., Beasley F.C., Liu S., Lajoie G.A., Heinrichs D.E.;
RT "Molecular characterization of staphyloferrin B biosynthesis in
RT Staphylococcus aureus.";
RL Mol. Microbiol. 74:594-608(2009).
CC -!- FUNCTION: Catalyzes the decarboxylation of citryl-L-2,3-
CC diaminopropionic acid to citryl-diaminoethane, the second step in
CC staphyloferrin B biosynthesis. {ECO:0000269|PubMed:19775248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate +
CC H(+) = 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate + CO2;
CC Xref=Rhea:RHEA:59120, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:142969, ChEBI:CHEBI:142970; EC=4.1.1.117;
CC Evidence={ECO:0000269|PubMed:19775248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59121;
CC Evidence={ECO:0000269|PubMed:19775248};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:19775248};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:19775248}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19775248}.
CC -!- INDUCTION: Up-regulated under iron-deficient growth conditions.
CC Repressed by Fur under iron-rich growth conditions.
CC {ECO:0000269|PubMed:14688077}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
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DR EMBL; AY251022; AAP82070.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29265.1; -; Genomic_DNA.
DR RefSeq; WP_001223700.1; NZ_LS483365.1.
DR RefSeq; YP_498682.1; NC_007795.1.
DR AlphaFoldDB; Q2G1M6; -.
DR SMR; Q2G1M6; -.
DR STRING; 1280.SAXN108_0110; -.
DR EnsemblBacteria; ABD29265; ABD29265; SAOUHSC_00082.
DR EnsemblBacteria; KXA40241; KXA40241; HMPREF3211_00226.
DR EnsemblBacteria; SUL22237; SUL22237; NCTC10654_00153.
DR EnsemblBacteria; SUL30549; SUL30549; NCTC10702_00272.
DR GeneID; 3919460; -.
DR KEGG; sao:SAOUHSC_00082; -.
DR PATRIC; fig|1280.3350.peg.101; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_0_3_9; -.
DR OMA; NISHHDF; -.
DR BioCyc; MetaCyc:G1I0R-76-MON; -.
DR BRENDA; 4.1.1.117; 3352.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR GO; GO:0019290; P:siderophore biosynthetic process; IDA:UniProtKB.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR002433; Orn_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..400
FT /note="2-[(L-alanin-3-ylcarbamoyl)methyl]-2-
FT hydroxybutanedioate decarboxylase"
FT /id="PRO_0000447128"
FT ACT_SITE 344
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00861"
FT BINDING 228
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P00861"
FT BINDING 266..269
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P00861"
FT BINDING 373
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P00861"
FT MOD_RES 50
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00861"
SQ SEQUENCE 400 AA; 45760 MW; DEB64CFADD47A837 CRC64;
MRIVQPVIEQ LKAQSHPVCH YIYDLVGLEH HLQHITSSLP SNCQMYYAMK ANSERKILDT
ISQYVEGFEV ASQGEIAKGL AFKPANHIIF GGPGKTDEEL RYAVSEGVQR IHVESMHELQ
RLNAILEDED KTQHILLRVN LAGPFPNATL HMAGRPTQFG ISEDEVDDVI EAALAMPKIH
LDGFHFHSIS NNLDSNLHVD VVKLYFKKAK AWSEKHRFPL KHINLGGGIG VNYADLTNQF
EWDNFVERFK TLIVEQEMED VTLNFECGRF IVAHIGYYVT EVLDIKKVHG AWYAILRGGT
QQFRLPVSWQ HNHPFDIYRY KDNPYSFEKV SISRQDTTLV GQLCTPKDVF AREVQIDAIS
TGDVIVFKYA GAYGWSISHH DFLSHPHPEF IYLTQTKEDE
