ODH_PSEAB
ID ODH_PSEAB Reviewed; 433 AA.
AC A0A0H2ZH12;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Pseudopaline synthase {ECO:0000305|PubMed:29214991};
DE EC=1.5.1.- {ECO:0000269|PubMed:29214991};
DE AltName: Full=Opine dehydrogenase;
DE Short=ODH;
DE AltName: Full=Pseudopaline dehydrogenase;
GN Name=cntM {ECO:0000303|PubMed:29214991};
GN Synonyms=zrmC {ECO:0000303|PubMed:28898501};
GN OrderedLocusNames=PA14_63920 {ECO:0000312|EMBL:ABJ14219.1};
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, AND
RP INTERACTION WITH CNTL.
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 NADH-dependent reductive condensation of alpha-
CC ketoglutarate to the intermediate formed by the adjacently encoded
CC enzyme CntL, namely (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-
CC yl)ethyl]amino}butanoate, leading to the production of pseudopaline.
CC This is the last step in the biosynthesis of the metallophore
CC pseudopaline, which is involved in the acquisition of nickel and zinc,
CC and thus enables bacterial growth inside the host, where metal access
CC is limited. Therefore, this enzyme probably contributes to Pseudomonas
CC virulence. Can use neither pyruvate nor NADPH in place of alpha-
CC ketoglutarate and NADH, respectively. {ECO:0000269|PubMed:29214991}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + pseudopaline = (2S)-2-amino-4-{[(1S)-1-carboxy-
CC 2-(1H-imidazol-4-yl)ethyl]amino}butanoate + 2-oxoglutarate + H(+) +
CC NADH; Xref=Rhea:RHEA:59788, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:143196, ChEBI:CHEBI:143198;
CC Evidence={ECO:0000269|PubMed:29214991};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:59790;
CC Evidence={ECO:0000305|PubMed:29214991};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CntL
CC (PubMed:29214991). {ECO:0000250|UniProtKB:Q9HUX5,
CC ECO:0000269|PubMed:29214991}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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 -!- SIMILARITY: Belongs to the staphylopine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ14219.1; -; Genomic_DNA.
DR RefSeq; WP_003095356.1; NZ_CP034244.1.
DR AlphaFoldDB; A0A0H2ZH12; -.
DR SMR; A0A0H2ZH12; -.
DR EnsemblBacteria; ABJ14219; ABJ14219; PA14_63920.
DR KEGG; pau:PA14_63920; -.
DR HOGENOM; CLU_637619_0_0_6; -.
DR OMA; RMPKEDY; -.
DR BioCyc; PAER208963:G1G74-5405-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016935; Opine_metallophore_DH.
DR Pfam; PF10100; Staph_opine_DH; 1.
DR PIRSF; PIRSF029692; UCP029692; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; NAD; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..433
FT /note="Pseudopaline synthase"
FT /id="PRO_0000447040"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 219
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8CKU7"
FT BINDING 16..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9HUX5"
FT BINDING 39..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9HUX5"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9HUX5"
FT BINDING 364
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9HUX5"
SQ SEQUENCE 433 AA; 47699 MW; 816BCABAD1F0BAF5 CRC64;
MNAADESLGN VLLVGLGAVA IQVALDLRRH GAGRLGALNH PGRRSQRIAE ALARGACLQL
EGQGQHRWLS GNAALDVFHQ DPAELRDDWQ TLVLCVPADS YLDVVRGLPW ERLGGVRTLL
LVSAFIGANL LVRSALPAGC QATVLSLSSY YAATKVIDET QPLRALTKAV KRRVYLGSSR
PDCPARETWR RVLAGSGVEV VPLATPEAAE GRNVTTYVHS PFFLGEFALA RILSEQGPPG
FMYKLYPEGP ITPGAIGAMR RLWCELSELL RRMGAEPLNL LRFLNDDNYP VHETMLPRAA
IDGFAEAGAE RQEYLLFVRY AALLVDPFSP ADEQGRHFDF SAVPFRRVSR DEDGLWRLPR
VPLEDYRKLA LIVALAAHFD LAMPQARSLL ASYENAVSRF IDCQGASQCH PSLYPIDSRP
AADAIYRQWC STC
