NASLL_PSEAB
ID NASLL_PSEAB Reviewed; 263 AA.
AC A0A0H2ZHV3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=L-histidine 2-aminobutanoyltransferase {ECO:0000305|PubMed:29214991};
DE EC=2.5.1.- {ECO:0000269|PubMed:29214991};
DE AltName: Full=Nicotianamine synthase-like enzyme;
DE Short=NAS;
GN Name=cntL {ECO:0000303|PubMed:29214991};
GN Synonyms=zrmB {ECO:0000303|PubMed:28898501};
GN OrderedLocusNames=PA14_63940 {ECO:0000312|EMBL:ABJ14220.1};
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP INDUCTION.
RC STRAIN=UCBPP-PA14;
RX PubMed=28898501; DOI=10.1111/mmi.13834;
RA Mastropasqua M.C., D'Orazio M., Cerasi M., Pacello F., Gismondi A.,
RA Canini A., Canuti L., Consalvo A., Ciavardelli D., Chirullo B.,
RA Pasquali P., Battistoni A.;
RT "Growth of Pseudomonas aeruginosa in zinc poor environments is promoted by
RT a nicotianamine-related metallophore.";
RL Mol. Microbiol. 106:543-561(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION, DISRUPTION
RP PHENOTYPE, AND INTERACTION WITH CNTM.
RC STRAIN=UCBPP-PA14;
RX PubMed=29214991; DOI=10.1038/s41598-017-16765-9;
RA Lhospice S., Gomez N.O., Ouerdane L., Brutesco C., Ghssein G., Hajjar C.,
RA Liratni A., Wang S., Richaud P., Bleves S., Ball G., Borezee-Durant E.,
RA Lobinski R., Pignol D., Arnoux P., Voulhoux R.;
RT "Pseudomonas aeruginosa zinc uptake in chelating environment is primarily
RT mediated by the metallophore pseudopaline.";
RL Sci. Rep. 7:17132-17132(2017).
CC -!- FUNCTION: Catalyzes the nucleophilic attack of one alpha-aminobutanoate
CC moiety from SAM onto L-histidine to produce the intermediate (2S)-2-
CC amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate.
CC Functions in the biosynthesis of the metallophore pseudopaline, which
CC is involved in the acquisition of nickel and zinc, and thus enables
CC bacterial growth inside the host, where metal access is limited.
CC Therefore, this enzyme probably contributes to Pseudomonas virulence.
CC Cannot use D-histidine in place of L-histidine as substrate.
CC {ECO:0000269|PubMed:29214991}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine + S-adenosyl-L-methionine = (2S)-2-amino-4-{[(1S)-
CC 1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H(+) + S-
CC methyl-5'-thioadenosine; Xref=Rhea:RHEA:59780, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17509, ChEBI:CHEBI:57595, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:143196; Evidence={ECO:0000269|PubMed:29214991};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59781;
CC Evidence={ECO:0000269|PubMed:29214991};
CC -!- SUBUNIT: Interacts with CntM. {ECO:0000269|PubMed:29214991}.
CC -!- INDUCTION: Is part of the operon cntOLMI that is negatively regulated
CC by zinc level through the Zur repressor, which leads to transcriptional
CC activation of this operon under zinc depletion.
CC {ECO:0000269|PubMed:28898501, ECO:0000269|PubMed:29214991}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to synthesize
CC pseudopaline and are impaired in their ability to import nickel in a
CC minimal media, supplemented or not with nickel. Under more stringent
CC conditions where a chelator such as EDTA is added to a minimal
CC succinate (MS) medium, a condition that presumably mimics the chelating
CC environment prevailing within a host or in airway mucus secretion
CC (AMS), the deletion mutant strain is unable to import zinc, therefore
CC reconciling the regulation of this operon by zinc with its function as
CC a zinc importer operating in metal scarce conditions.
CC {ECO:0000269|PubMed:29214991}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CntL family.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ14220.1; -; Genomic_DNA.
DR RefSeq; WP_003095359.1; NZ_CP034244.1.
DR AlphaFoldDB; A0A0H2ZHV3; -.
DR SMR; A0A0H2ZHV3; -.
DR EnsemblBacteria; ABJ14220; ABJ14220; PA14_63940.
DR KEGG; pau:PA14_63940; -.
DR HOGENOM; CLU_089313_0_0_6; -.
DR OMA; EARMQFS; -.
DR BioCyc; PAER208963:G1G74-5406-MON; -.
DR Proteomes; UP000000653; 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 Pfam; PF03059; NAS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..263
FT /note="L-histidine 2-aminobutanoyltransferase"
FT /id="PRO_0000447036"
SQ SEQUENCE 263 AA; 28932 MW; CFD5C4492154E953 CRC64;
MQGRTPLLET LRELECEIRL LTVYARECCG CYEILRRKLD RLSGLIGEDC SRAQWQADSD
DPALQALGLR LRDAAVQALC ELEKHLCQGV LHEPGEMGRY LGSLLESIRG ELDSAGIDAD
ARVLFVGSGA LPTSALVLAR EVGAHLCCLD IDEEALGYAR EIARCQGLEA RMQFSSLPPA
ELAFSRDATH FLIASLVQQK SAVLAQIRQV MRADAKVLLR HGSGIKGLFN YPVEPAELEG
WQVCAERVSQ PLYDTLILEK AGR
