SHDHL_HAEIN
ID SHDHL_HAEIN Reviewed; 271 AA.
AC P44774;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Shikimate dehydrogenase-like protein HI_0607 {ECO:0000303|PubMed:15735308};
DE Short=SDH-L {ECO:0000303|PubMed:15735308};
DE EC=1.1.1.25 {ECO:0000269|PubMed:15735308};
GN Name=sdhL {ECO:0000303|PubMed:25524738}; OrderedLocusNames=HI_0607;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP REVIEW, REACTION MECHANISM, AND ACTIVE SITE.
RX PubMed=25524738; DOI=10.1016/j.abb.2014.12.006;
RA Peek J., Christendat D.;
RT "The shikimate dehydrogenase family: functional diversity within a
RT conserved structural and mechanistic framework.";
RL Arch. Biochem. Biophys. 566:85-99(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, MUTAGENESIS OF LYS-67
RP AND ASP-103, AND SUBUNIT.
RX PubMed=15735308; DOI=10.1074/jbc.m412753200;
RA Singh S., Korolev S., Koroleva O., Zarembinski T., Collart F.,
RA Joachimiak A., Christendat D.;
RT "Crystal structure of a novel shikimate dehydrogenase from Haemophilus
RT influenzae.";
RL J. Biol. Chem. 280:17101-17108(2005).
CC -!- FUNCTION: In vitro, is able to catalyze the NADP(+)-dependent oxidation
CC of shikimate to 3-dehydroshikimate. However, has much lower activity
CC than classical shikimate dehydrogenases AroE, indicating that shikimate
CC may not be the biological substrate. Cannot utilize NAD(+) instead of
CC NADP(+). Is not able to catalyze the oxidation of quinate.
CC {ECO:0000269|PubMed:15735308}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC Evidence={ECO:0000269|PubMed:15735308};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=234 uM for shikimate {ECO:0000269|PubMed:15735308};
CC KM=234 uM for NADP(+) {ECO:0000269|PubMed:15735308};
CC Note=kcat is 0.2 sec(-1). {ECO:0000269|PubMed:15735308};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:15735308};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15735308}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase-like family.
CC {ECO:0000305|PubMed:15735308, ECO:0000305|PubMed:25524738}.
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DR EMBL; L42023; AAC22266.1; -; Genomic_DNA.
DR PIR; H64080; H64080.
DR RefSeq; NP_438765.1; NC_000907.1.
DR RefSeq; WP_005694543.1; NC_000907.1.
DR PDB; 1NPY; X-ray; 1.75 A; A/B/C/D=1-271.
DR PDBsum; 1NPY; -.
DR AlphaFoldDB; P44774; -.
DR SMR; P44774; -.
DR STRING; 71421.HI_0607; -.
DR EnsemblBacteria; AAC22266; AAC22266; HI_0607.
DR KEGG; hin:HI_0607; -.
DR PATRIC; fig|71421.8.peg.631; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_3_0_6; -.
DR OMA; MPFKESC; -.
DR PhylomeDB; P44774; -.
DR BioCyc; HINF71421:G1GJ1-626-MON; -.
DR BRENDA; 1.1.1.282; 2529.
DR EvolutionaryTrace; P44774; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..271
FT /note="Shikimate dehydrogenase-like protein HI_0607"
FT /id="PRO_0000136073"
FT ACT_SITE 67
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:25524738"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:25524738"
FT BINDING 126..130
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P43876"
FT BINDING 154
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P43876"
FT BINDING 184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P43876"
FT MUTAGEN 67
FT /note="K->A,H,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15735308"
FT MUTAGEN 103
FT /note="D->A,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15735308"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1NPY"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1NPY"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1NPY"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:1NPY"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 235..251
FT /evidence="ECO:0007829|PDB:1NPY"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:1NPY"
SQ SEQUENCE 271 AA; 29932 MW; A7A6AC9B9388394E CRC64;
MINKDTQLCM SLSGRPSNFG TTFHNYLYDK LGLNFIYKAF TTQDIEHAIK GVRALGIRGC
AVSMPFKETC MPFLDEIHPS AQAIESVNTI VNDNGFLRAY NTDYIAIVKL IEKYHLNKNA
KVIVHGSGGM AKAVVAAFKN SGFEKLKIYA RNVKTGQYLA ALYGYAYINS LENQQADILV
NVTSIGMKGG KEEMDLAFPK AFIDNASVAF DVVAMPVETP FIRYAQARGK QTISGAAVIV
LQAVEQFELY THQRPSDELI AEAAAFARTK F
