ODH_STAAM
ID ODH_STAAM Reviewed; 433 AA.
AC A0A0H3JT80;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Staphylopine synthase {ECO:0000305|PubMed:27230378};
DE EC=1.5.1.52 {ECO:0000269|PubMed:27230378, ECO:0000269|PubMed:29091735, ECO:0000269|PubMed:29618515};
DE AltName: Full=Opine dehydrogenase {ECO:0000303|PubMed:29091735, ECO:0000303|PubMed:29618515};
DE Short=ODH {ECO:0000303|PubMed:29091735, ECO:0000303|PubMed:29618515};
DE AltName: Full=Staphylopine dehydrogenase {ECO:0000303|PubMed:29618515};
GN Name=cntM {ECO:0000303|PubMed:27230378};
GN OrderedLocusNames=SAV2468 {ECO:0000312|EMBL:BAB58630.1};
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, SUBSTRATE SPECIFICITY, AND INDUCTION.
RC STRAIN=Mu50 / ATCC 700699;
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, AND SUBSTRATE 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).
RN [4] {ECO:0007744|PDB:6C4R, ECO:0007744|PDB:6C4T}
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP NADP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=29618515; DOI=10.1074/jbc.ra118.002007;
RA McFarlane J.S., Davis C.L., Lamb A.L.;
RT "Staphylopine, pseudopaline, and yersinopine dehydrogenases: A structural
RT and kinetic analysis of a new functional class of opine dehydrogenase.";
RL J. Biol. Chem. 293:8009-8019(2018).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reductive condensation of
CC pyruvate to the intermediate formed by the adjacently encoded enzyme
CC CntL, namely (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-
CC yl)ethyl]amino}butanoate, leading to the production of staphylopine.
CC This is the last step in the biosynthesis of the metallophore
CC staphylopine, which is involved in the acquisition of nickel, cobalt,
CC zinc, copper, and iron, and thus enables bacterial growth inside the
CC host, where metal access is limited. Therefore, this enzyme probably
CC contributes to staphylococcal virulence. Can use neither NADH nor
CC alpha-ketoglutarate in place of NADPH and pyruvate, respectively.
CC {ECO:0000269|PubMed:27230378, ECO:0000269|PubMed:29091735,
CC ECO:0000269|PubMed:29618515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + staphylopine = (2S)-2-amino-4-{[(1R)-1-
CC carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H(+) + NADPH +
CC pyruvate; Xref=Rhea:RHEA:57508, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:141669, ChEBI:CHEBI:141808; EC=1.5.1.52;
CC Evidence={ECO:0000269|PubMed:27230378, ECO:0000269|PubMed:29091735,
CC ECO:0000269|PubMed:29618515};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57510;
CC Evidence={ECO:0000305|PubMed:27230378, ECO:0000305|PubMed:29091735};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for pyruvate (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:29618515};
CC KM=1400 uM for oxaloacetate (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:29618515};
CC KM=3000 uM for glyoxylate (at pH 8.0 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:29618515};
CC Note=kcat is 0.26 sec(-1) with pyruvate as substrate. kcat is 0.26
CC sec(-1) with oxaloacetate as substrate. kcat is 0.074 sec(-1) with
CC glyoxylate as substrate (at pH 8.0 and 22 degrees Celsius).
CC {ECO:0000269|PubMed:29618515};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29618515}.
CC -!- INDUCTION: Up-regulated in metal-poor media.
CC {ECO:0000269|PubMed:27230378}.
CC -!- SIMILARITY: Belongs to the staphylopine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BA000017; BAB58630.1; -; Genomic_DNA.
DR RefSeq; WP_000040588.1; NC_002758.2.
DR PDB; 6C4R; X-ray; 2.29 A; A=1-433.
DR PDB; 6C4T; X-ray; 2.49 A; A=1-433.
DR PDB; 6GMZ; X-ray; 2.22 A; A=1-433.
DR PDB; 6H31; X-ray; 2.30 A; A/B=1-433.
DR PDB; 6H3D; X-ray; 2.05 A; A=1-433.
DR PDB; 6H3F; X-ray; 2.21 A; A=1-433.
DR PDBsum; 6C4R; -.
DR PDBsum; 6C4T; -.
DR PDBsum; 6GMZ; -.
DR PDBsum; 6H31; -.
DR PDBsum; 6H3D; -.
DR PDBsum; 6H3F; -.
DR AlphaFoldDB; A0A0H3JT80; -.
DR SMR; A0A0H3JT80; -.
DR PaxDb; A0A0H3JT80; -.
DR EnsemblBacteria; BAB58630; BAB58630; SAV2468.
DR KEGG; sav:SAV2468; -.
DR HOGENOM; CLU_637619_0_0_9; -.
DR OMA; RMPKEDY; -.
DR BioCyc; SAUR158878:SAV_RS13470-MON; -.
DR BRENDA; 1.5.1.52; 3352.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR016935; Opine_metallophore_DH.
DR Pfam; PF10100; Staph_opine_DH; 1.
DR PIRSF; PIRSF029692; UCP029692; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase.
FT CHAIN 1..433
FT /note="Staphylopine synthase"
FT /id="PRO_0000447038"
FT ACT_SITE 216
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8CKU7"
FT BINDING 9..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29618515"
FT BINDING 33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29618515"
FT BINDING 37..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29618515"
FT BINDING 99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29618515"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:6H3D"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 250..269
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:6H3D"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 357..375
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 381..400
FT /evidence="ECO:0007829|PDB:6H3D"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:6H3D"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:6H3D"
FT HELIX 416..428
FT /evidence="ECO:0007829|PDB:6H3D"
SQ SEQUENCE 433 AA; 50072 MW; F7E21B62F56957F8 CRC64;
MSKLLMIGTG PVAIQLANIC YLKSDYEIDM VGRASTSEKS KRLYQAYKKE KQFEVKIQNE
AHQHLEGKFE INRLYKDVKN VKGEYETVVM ACTADAYYDT LQQLSLETLQ SVKHVILISP
TFGSQMIVEQ FMSKFSQDIE VISFSTYLGD TRIVDKEAPN HVLTTGVKKK LYMGSTHSNS
TMCQRISALA EQLKIQLEVV ESPLHAETRN SSLYVHPPLF MNDFSLKAIF EGTDVPVYVY
KLFPEGPITM TLIREMRLMW KEMMAILQAF RVPSVNLLQF MVKENYPVRP ETLDEGDIEH
FEILPDILQE YLLYVRYTAI LIDPFSQPDE NGHYFDFSAV PFKQVYKNEQ DVVQIPRMPS
EDYYRTAMIQ HIGKMLGIKT PMIDQFLTRY EASCQAYKDM HQDQQLSSQF NTNLFEGDKA
LVTKFLEINR TLS
