SBNB_STAA8
ID SBNB_STAA8 Reviewed; 336 AA.
AC Q2G1N2; Q6X7U6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=N-((2S)-2-amino-2-carboxyethyl)-L-glutamate dehydrogenase {ECO:0000305};
DE EC=1.5.1.51 {ECO:0000269|PubMed:24485762};
DE AltName: Full=Staphyloferrin B biosynthesis protein SbnB {ECO:0000305};
GN Name=sbnB {ECO:0000303|PubMed:14688077};
GN OrderedLocusNames=SAOUHSC_00076 {ECO:0000312|EMBL:ABD29259.1};
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 PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=21906287; DOI=10.1186/1471-2180-11-199;
RA Beasley F.C., Cheung J., Heinrichs D.E.;
RT "Mutation of L-2,3-diaminopropionic acid synthase genes blocks
RT staphyloferrin B synthesis in Staphylococcus aureus.";
RL BMC Microbiol. 11:199-199(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=24485762; DOI=10.1016/j.chembiol.2013.12.011;
RA Kobylarz M.J., Grigg J.C., Takayama S.J., Rai D.K., Heinrichs D.E.,
RA Murphy M.E.;
RT "Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic
RT precursor.";
RL Chem. Biol. 21:379-388(2014).
CC -!- FUNCTION: Catalyzes the hydrolysis of N-((2S)-2-amino-2-carboxyethyl)-
CC L-glutamate (ACEGA) to form L-2,3-diaminopropionic acid and 2-
CC oxoglutarate. Involved in the biosynthesis of L-2,3-diaminopropionic
CC acid (L-Dap), a precursor of staphyloferrin B and antibiotics.
CC {ECO:0000269|PubMed:24485762}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD(+) =
CC (S)-2,3-diaminopropanoate + 2-oxoglutarate + H(+) + NADH;
CC Xref=Rhea:RHEA:51928, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57721,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:134610; EC=1.5.1.51;
CC Evidence={ECO:0000269|PubMed:24485762};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51929;
CC Evidence={ECO:0000269|PubMed:24485762};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:21906287}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24485762}.
CC -!- INDUCTION: Up-regulated under iron-deficient growth conditions.
CC Repressed by Fur under iron-rich growth conditions.
CC {ECO:0000269|PubMed:14688077}.
CC -!- DISRUPTION PHENOTYPE: Mutation results in abrogation of synthesis of
CC staphyloferrin B. {ECO:0000269|PubMed:21906287}.
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. {ECO:0000305}.
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DR EMBL; AY251022; AAP82064.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29259.1; -; Genomic_DNA.
DR RefSeq; WP_001078456.1; NZ_LS483365.1.
DR RefSeq; YP_498676.1; NC_007795.1.
DR AlphaFoldDB; Q2G1N2; -.
DR SMR; Q2G1N2; -.
DR STRING; 1280.SAXN108_0103; -.
DR EnsemblBacteria; ABD29259; ABD29259; SAOUHSC_00076.
DR EnsemblBacteria; CRI17543; CRI17543; BN1321_40041.
DR EnsemblBacteria; KXA40235; KXA40235; HMPREF3211_00220.
DR EnsemblBacteria; PPJ75762; PPJ75762; CV021_04085.
DR EnsemblBacteria; PPJ93938; PPJ93938; CSC83_08590.
DR EnsemblBacteria; PPK15808; PPK15808; CSC87_03805.
DR EnsemblBacteria; SCT49673; SCT49673; SAMEA1708674_03203.
DR EnsemblBacteria; SCT50026; SCT50026; SAMEA1708674_03214.
DR EnsemblBacteria; SCT50207; SCT50207; SAMEA1708674_03220.
DR EnsemblBacteria; SUK27788; SUK27788; NCTC6133_00085.
DR EnsemblBacteria; SUL22161; SUL22161; NCTC10654_00147.
DR EnsemblBacteria; SUL30542; SUL30542; NCTC10702_00265.
DR GeneID; 3919454; -.
DR KEGG; sao:SAOUHSC_00076; -.
DR PATRIC; fig|1280.10758.peg.90; -.
DR eggNOG; COG2423; Bacteria.
DR HOGENOM; CLU_042088_3_1_9; -.
DR OMA; DMIEPGM; -.
DR BioCyc; MetaCyc:G1I0R-70-MON; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0019290; P:siderophore biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.30.1780.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR InterPro; IPR023866; SbnB.
DR PANTHER; PTHR13812; PTHR13812; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03944; dehyd_SbnB_fam; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..336
FT /note="N-((2S)-2-amino-2-carboxyethyl)-L-glutamate
FT dehydrogenase"
FT /id="PRO_0000447129"
FT ACT_SITE 78
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O28608"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O28608"
FT BINDING 242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O28608"
SQ SEQUENCE 336 AA; 37749 MW; CCC2F43BE1505979 CRC64;
MNREMLYLNR SDIEQAGGNH SQVYVDALTE ALTAHAHNDF VQPLKPYLRQ DPENGHIADR
IIAMPSHIGG EHAISGIKWI GSKHDNPSKR NMERASGVII LNDPETNYPI AVMEASLISS
MRTAAVSVIA AKHLAKKGFK DLTIIGCGLI GDKQLQSMLE QFDHIERVFV YDQFSEACAR
FVDRWQQQRP EINFIATENA KEAVSNGEVV ITCTVTDQPY IEYDWLQKGA FISNISIMDV
HKEVFIKADK VVVDDWSQCN REKKTINQLV LEGKFSKEAL HAELGQLVTG DIPGREDDDE
IILLNPMGMA IEDISSAYFI YQQAQQQNIG TTLNLY
