NASLD_STAAM
ID NASLD_STAAM Reviewed; 272 AA.
AC A0A0H3JXA8;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=D-histidine 2-aminobutanoyltransferase {ECO:0000305|PubMed:27230378};
DE EC=2.5.1.152 {ECO:0000269|PubMed:27230378, ECO:0000269|PubMed:29091735};
DE AltName: Full=Nicotianamine synthase-like enzyme {ECO:0000303|PubMed:27230378};
DE Short=NAS {ECO:0000303|PubMed:27230378, ECO:0000303|PubMed:29091735};
GN Name=cntL {ECO:0000303|PubMed:27230378};
GN OrderedLocusNames=SAV2469 {ECO:0000312|EMBL:BAB58631.1};
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SAM-BINDING, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Mu50 / ATCC 700699, and RN6390;
RX PubMed=27230378; DOI=10.1126/science.aaf1018;
RA Ghssein G., Brutesco C., Ouerdane L., Fojcik C., Izaute A., Wang S.,
RA Hajjar C., Lobinski R., Lemaire D., Richaud P., Voulhoux R., Espaillat A.,
RA Cava F., Pignol D., Borezee-Durant E., Arnoux P.;
RT "Biosynthesis of a broad-spectrum nicotianamine-like metallophore in
RT Staphylococcus aureus.";
RL Science 352:1105-1109(2016).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=29091735; DOI=10.1021/acs.biochem.7b00804;
RA McFarlane J.S., Lamb A.L.;
RT "Biosynthesis of an Opine Metallophore by Pseudomonas aeruginosa.";
RL Biochemistry 56:5967-5971(2017).
CC -!- FUNCTION: Catalyzes the nucleophilic attack of one alpha-aminobutanoate
CC moiety from SAM onto D-histidine to produce the intermediate (2S)-2-
CC amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate.
CC Functions in the biosynthesis of the metallophore staphylopine, which
CC is involved in the acquisition of nickel, cobalt, zinc, copper, and
CC iron, and thus enables bacterial growth inside the host, where metal
CC access is limited. Therefore, this enzyme probably contributes to
CC staphylococcal virulence (PubMed:27230378, PubMed:29091735). Appears to
CC be specific for D-histidine as substrate (PubMed:29091735).
CC {ECO:0000269|PubMed:27230378, ECO:0000269|PubMed:29091735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-histidine + S-adenosyl-L-methionine = (2S)-2-amino-4-{[(1R)-
CC 1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H(+) + S-
CC methyl-5'-thioadenosine; Xref=Rhea:RHEA:59088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:141808,
CC ChEBI:CHEBI:142967; EC=2.5.1.152;
CC Evidence={ECO:0000269|PubMed:27230378, ECO:0000269|PubMed:29091735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59089;
CC Evidence={ECO:0000269|PubMed:27230378, ECO:0000305|PubMed:29091735};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.0 uM for D-histidine {ECO:0000269|PubMed:29091735};
CC Note=kcat is 1.79 min(-1). {ECO:0000269|PubMed:29091735};
CC -!- INDUCTION: Up-regulated in metal-poor media.
CC {ECO:0000269|PubMed:27230378}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce neither
CC staphylopine nor the biosynthetic intermediate 2-amino-4-{[1-carboxy-2-
CC (1H-imidazol-4-yl)ethyl]amino}butanoate. They also show a decrease in
CC the intracellular content of nickel, copper, cobalt, iron, and zinc.
CC {ECO:0000269|PubMed:27230378}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CntL family.
CC {ECO:0000305}.
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DR EMBL; BA000017; BAB58631.1; -; Genomic_DNA.
DR RefSeq; WP_001058848.1; NC_002758.2.
DR AlphaFoldDB; A0A0H3JXA8; -.
DR SMR; A0A0H3JXA8; -.
DR PaxDb; A0A0H3JXA8; -.
DR EnsemblBacteria; BAB58631; BAB58631; SAV2469.
DR KEGG; sav:SAV2469; -.
DR HOGENOM; CLU_089313_0_0_9; -.
DR OMA; EARMQFS; -.
DR BioCyc; SAUR158878:SAV_RS13475-MON; -.
DR BRENDA; 2.5.1.152; 3352.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0030410; F:nicotianamine synthase activity; IEA:InterPro.
DR GO; GO:0030418; P:nicotianamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004298; Nicotian_synth.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR32266; PTHR32266; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..272
FT /note="D-histidine 2-aminobutanoyltransferase"
FT /id="PRO_0000447034"
SQ SEQUENCE 272 AA; 31126 MW; A07BE5BFD02D4D55 CRC64;
MNNFNNEIKL ILQQYLEKFE AHYERVLQDD QYIEALETLM DDYSEFILNP IYEQQFNAWR
DVEEKAQLIK SLQYITAQCV KQVEVIRARR LLDGQASTTG YFDNIEHCID EEFGQCSITS
NDKLLLVGSG AYPMTLIQVA KETGASVIGI DIDPQAVDLG RRIVNVLAPN EDITITDQKV
SELKDIKDVT HIIFSSTIPL KYSILEELYD LTNENVVVAM RFGDGIKAIF NYPSQETAED
KWQCVNKHMR PQQIFDIALY KKAAIKVGIT DV
