SERDH_PSEAE
ID SERDH_PSEAE Reviewed; 298 AA.
AC Q9I5I6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=NAD-dependent L-serine dehydrogenase;
DE EC=1.1.1.387 {ECO:0000269|PubMed:22128181};
DE AltName: Full=L-serine 3-dehydrogenase (NAD(+));
GN OrderedLocusNames=PA0743;
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 X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE,
RP AND MUTAGENESIS OF THR-96; SER-122; ASN-175; TRP-214; TYR-219; LYS-246 AND
RP ASP-247.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=22128181; DOI=10.1074/jbc.m111.294561;
RA Tchigvintsev A., Singer A., Brown G., Flick R., Evdokimova E., Tan K.,
RA Gonzalez C.F., Savchenko A., Yakunin A.F.;
RT "Biochemical and structural studies of uncharacterized protein PA0743 from
RT Pseudomonas aeruginosa revealed NAD+-dependent L-serine dehydrogenase.";
RL J. Biol. Chem. 287:1874-1883(2012).
CC -!- FUNCTION: NAD-dependent L-serine dehydrogenase that catalyzes the
CC oxidation of L-serine and methyl-L-serine and is possibly involved in
CC serine catabolism. Has low activity toward beta-hydroxyisobutyrate.
CC {ECO:0000269|PubMed:22128181}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine + NAD(+) = aminoacetaldehyde + CO2 + NADH;
CC Xref=Rhea:RHEA:43628, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58213;
CC EC=1.1.1.387; Evidence={ECO:0000269|PubMed:22128181};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 mM for L-serine {ECO:0000269|PubMed:22128181};
CC KM=2.4 mM for methyl-DL-serine {ECO:0000269|PubMed:22128181};
CC KM=19.8 mM for DL-glycerate {ECO:0000269|PubMed:22128181};
CC KM=17.4 mM for methyl-2,2-dimethyl-3-hydroxypropionate
CC {ECO:0000269|PubMed:22128181};
CC KM=3.4 mM for NAD {ECO:0000269|PubMed:22128181};
CC Vmax=18.7 umol/min/mg enzyme with L-serine as substrate
CC {ECO:0000269|PubMed:22128181};
CC Vmax=17.2 umol/min/mg enzyme with methyl-DL-serine as substrate
CC {ECO:0000269|PubMed:22128181};
CC Vmax=10.4 umol/min/mg enzyme with DL-glycerate as substrate
CC {ECO:0000269|PubMed:22128181};
CC Vmax=20.9 umol/min/mg enzyme with methyl-2,2-dimethyl-3-
CC hydroxypropionate as substrate {ECO:0000269|PubMed:22128181};
CC Vmax=2.8 umol/min/mg enzyme with NAD as substrate
CC {ECO:0000269|PubMed:22128181};
CC Note=kcat is 10.4 sec(-1) with L-serine as substrate. kcat is 9.6
CC sec(-1) with methyl-DL-serine as substrate. kcat is 5.8 sec(-1) with
CC DL-glycerate as substrate. kcat is 11.6 sec(-1) with methyl-2,2-
CC dimethyl-3-hydroxypropionate as substrate. kcat is 1.6 sec(-1) with
CC NAD as substrate.;
CC -!- PATHWAY: Amino-acid degradation.
CC -!- SUBUNIT: Homotetramer, dimer of dimers. {ECO:0000269|PubMed:22128181}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04132.1; -; Genomic_DNA.
DR PIR; B83553; B83553.
DR RefSeq; NP_249434.1; NC_002516.2.
DR RefSeq; WP_003114168.1; NZ_QZGE01000007.1.
DR PDB; 3OBB; X-ray; 2.20 A; A=1-298.
DR PDB; 3Q3C; X-ray; 2.30 A; A=1-298.
DR PDBsum; 3OBB; -.
DR PDBsum; 3Q3C; -.
DR AlphaFoldDB; Q9I5I6; -.
DR SMR; Q9I5I6; -.
DR STRING; 287.DR97_1241; -.
DR PaxDb; Q9I5I6; -.
DR PRIDE; Q9I5I6; -.
DR EnsemblBacteria; AAG04132; AAG04132; PA0743.
DR GeneID; 882135; -.
DR KEGG; pae:PA0743; -.
DR PATRIC; fig|208964.12.peg.772; -.
DR PseudoCAP; PA0743; -.
DR HOGENOM; CLU_035117_6_0_6; -.
DR InParanoid; Q9I5I6; -.
DR OMA; AWVQSTT; -.
DR PhylomeDB; Q9I5I6; -.
DR BioCyc; PAER208964:G1FZ6-756-MON; -.
DR BRENDA; 1.1.1.387; 5087.
DR SABIO-RK; Q9I5I6; -.
DR EvolutionaryTrace; Q9I5I6; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006565; P:L-serine catabolic process; TAS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR011548; HIBADH.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01692; HIBADH; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Branched-chain amino acid catabolism; NAD;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..298
FT /note="NAD-dependent L-serine dehydrogenase"
FT /id="PRO_0000429132"
FT ACT_SITE 171
FT /evidence="ECO:0000269|PubMed:22128181"
FT BINDING 2..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22128181"
FT BINDING 65..66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22128181"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22128181"
FT BINDING 246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22128181"
FT MUTAGEN 96
FT /note="T->A: Almost abolished activity."
FT /evidence="ECO:0000269|PubMed:22128181"
FT MUTAGEN 122
FT /note="S->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:22128181"
FT MUTAGEN 171
FT /note="K->A: Strongly reduced activity."
FT MUTAGEN 175
FT /note="N->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:22128181"
FT MUTAGEN 214
FT /note="W->A: Almost abolished activity."
FT /evidence="ECO:0000269|PubMed:22128181"
FT MUTAGEN 219
FT /note="Y->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:22128181"
FT MUTAGEN 246
FT /note="K->A: Almost abolished activity."
FT /evidence="ECO:0000269|PubMed:22128181"
FT MUTAGEN 247
FT /note="D->A: Almost abolished activity."
FT /evidence="ECO:0000269|PubMed:22128181"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:3OBB"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 166..194
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:3OBB"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:3OBB"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 241..258
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:3OBB"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:3OBB"
SQ SEQUENCE 298 AA; 30754 MW; 27100627BEBB469C CRC64;
MKQIAFIGLG HMGAPMATNL LKAGYLLNVF DLVQSAVDGL VAAGASAARS ARDAVQGADV
VISMLPASQH VEGLYLDDDG LLAHIAPGTL VLECSTIAPT SARKIHAAAR ERGLAMLDAP
VSGGTAGAAA GTLTFMVGGD AEALEKARPL FEAMGRNIFH AGPDGAGQVA KVCNNQLLAV
LMIGTAEAMA LGVANGLEAK VLAEIMRRSS GGNWALEVYN PWPGVMENAP ASRDYSGGFM
AQLMAKDLGL AQEAAQASAS STPMGSLALS LYRLLLKQGY AERDFSVVQK LFDPTQGQ
