NASLL_PSEAE
ID NASLL_PSEAE Reviewed; 263 AA.
AC Q9HUX4;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=L-histidine 2-aminobutanoyltransferase {ECO:0000305|PubMed:29091735};
DE EC=2.5.1.- {ECO:0000269|PubMed:29091735};
DE AltName: Full=Nicotianamine synthase-like enzyme {ECO:0000305|PubMed:29091735};
DE Short=NAS {ECO:0000303|PubMed:29091735};
GN Name=cntL {ECO:0000250|UniProtKB:A0A0H2ZHV3};
GN Synonyms=zrmB {ECO:0000303|PubMed:28898501};
GN OrderedLocusNames=PA4836 {ECO:0000312|EMBL:AAG08221.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=26446565; DOI=10.1038/srep14644;
RA Gi M., Lee K.M., Kim S.C., Yoon J.H., Yoon S.S., Choi J.Y.;
RT "A novel siderophore system is essential for the growth of Pseudomonas
RT aeruginosa in airway mucus.";
RL Sci. Rep. 5:14644-14644(2015).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SAM-BINDING, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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 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 Appears to be specific for L-histidine as substrate.
CC {ECO:0000269|PubMed:29091735}.
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:29091735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59781;
CC Evidence={ECO:0000305|PubMed:29091735};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for L-histidine (at pH 8 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:29091735};
CC Note=kcat is 1.07 min(-1) (at pH 8 and 22 degrees Celsius).
CC {ECO:0000269|PubMed:29091735};
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 (PubMed:28898501).
CC Highly induced in response to airway mucus secretions (AMS) treatment
CC (PubMed:26446565). {ECO:0000269|PubMed:26446565,
CC ECO:0000269|PubMed:28898501}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CntL family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG08221.1; -; Genomic_DNA.
DR PIR; H83042; H83042.
DR RefSeq; NP_253523.1; NC_002516.2.
DR RefSeq; WP_003112332.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUX4; -.
DR SMR; Q9HUX4; -.
DR STRING; 287.DR97_2186; -.
DR PaxDb; Q9HUX4; -.
DR DNASU; 878136; -.
DR EnsemblBacteria; AAG08221; AAG08221; PA4836.
DR GeneID; 878136; -.
DR KEGG; pae:PA4836; -.
DR PATRIC; fig|208964.12.peg.5067; -.
DR PseudoCAP; PA4836; -.
DR HOGENOM; CLU_089313_0_0_6; -.
DR OMA; EARMQFS; -.
DR PhylomeDB; Q9HUX4; -.
DR BioCyc; PAER208964:G1FZ6-4950-MON; -.
DR Proteomes; UP000002438; 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 Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..263
FT /note="L-histidine 2-aminobutanoyltransferase"
FT /id="PRO_0000447035"
SQ SEQUENCE 263 AA; 28886 MW; 62B8F4861DA54BE2 CRC64;
MQGRTPLLET LRELECEIRL LTVYARECCG CYEILRRKLD RLSGLIGEDC SRAQWQADSD
DPALQALGLR LRDAAVQALC ELEKHLCQGV LHEPGEMGRY LGSLLESIRG ELDSAGIDAD
ARVLFVGSGA LPTSALVLAR EVGAHLCCLD IDEEALGCAR EIARCQGLEA RMQFSSLPPA
ELAFSRDATH FLIASLVQQK SAVLAQIRQV MRADAKVLLR HGSGIKGLFN YPVEPAELDG
WRVCAERVSQ PLYDTLILEK AGR
