Reviewed, UniProtKB/Swiss-Prot P44774 (Y607_HAEIN)

Names and origin

Protein names

Recommended name:
    Shikimate 5-dehydrogenase-like protein HI0607
      Short name=SDH-L
    EC=1.1.1.-

Gene names

Ordered Locus Names:

HI0607

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The physiological substrate is not known. Has much lower activity towards shikimate than aroE. Ref.2
Catalytic activity	Shikimate + NAD(P)+ = 3-dehydroshikimate + NADH. HAMAP MF_00222
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the shikimate dehydrogenase family.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	binding Inferred from electronic annotation. Source: InterPro shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 271

271

Shikimate 5-dehydrogenase-like protein HI0607 HAMAP MF_00222

PRO_0000136073

Regions

Nucleotide binding

126 – 130

5

NADP By similarity

Nucleotide binding

235 – 239

5

NADP By similarity

Sites

Active site

67

1

Proton acceptor Potential

Binding site

103

1

Substrate Probable

Experimental info

Mutagenesis

67

1

K → A, H or N: Loss of activity. Ref.2

Mutagenesis

103

1

D → A or N: Loss of activity. Ref.2

Secondary structure

1

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271

Helix Strand Turn

Details...

Beta strand

7 – 12

6

Helix

19 – 31

13

Beta strand

35 – 40

6

Helix

45 – 55

11

Beta strand

59 – 62

4

Turn

67 – 70

4

Helix

71 – 73

3

Beta strand

75 – 77

3

Helix

79 – 82

4

Turn

83 – 85

3

Beta strand

89 – 93

5

Beta strand

96 – 100

5

Helix

102 – 113

12

Beta strand

122 – 125

4

Helix

131 – 140

10

Beta strand

146 – 149

4

Helix

153 – 163

11

Beta strand

166 – 169

4

Beta strand

177 – 181

5

Turn

191 – 194

4

Helix

200 – 205

6

Beta strand

207 – 211

5

Beta strand

215 – 218

4

Helix

220 – 227

8

Beta strand

231 – 233

3

Helix

235 – 251

17

Helix

257 – 268

12

Sequences

	Sequence		Length	Mass (Da)
	P44774-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: A7A6AC9B9388394E	FASTA	271	29,932
	10 20 30 40 50 60 MINKDTQLCM SLSGRPSNFG TTFHNYLYDK LGLNFIYKAF TTQDIEHAIK GVRALGIRGC 70 80 90 100 110 120 AVSMPFKETC MPFLDEIHPS AQAIESVNTI VNDNGFLRAY NTDYIAIVKL IEKYHLNKNA 130 140 150 160 170 180 KVIVHGSGGM AKAVVAAFKN SGFEKLKIYA RNVKTGQYLA ALYGYAYINS LENQQADILV 190 200 210 220 230 240 NVTSIGMKGG KEEMDLAFPK AFIDNASVAF DVVAMPVETP FIRYAQARGK QTISGAAVIV 250 260 270 LQAVEQFELY THQRPSDELI AEAAAFARTK F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae." Singh S., Korolev S., Koroleva O., Zarembinski T., Collart F., Joachimiak A., Christendat D. J. Biol. Chem. 280:17101-17108(2005) [PubMed: 15735308] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), FUNCTION, MUTAGENESIS OF LYS-67 AND ASP-103, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L42023 Genomic DNA. Translation: AAC22266.1.

PIR

H64080.

RefSeq

NP_438765.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NPY	X-ray	1.75	A/B/C/D	1-271	[»]

ModBase

Search...

Genome annotation databases

GeneID

949659.

GenomeReviews

Gene locus HI0607 in contig L42023_GR.

KEGG

hin:HI0607.

NMPDR

fig|71421.1.peg.576.

TIGR

HI0607.

Phylogenomic databases

HOGENOM

P44774.

OMA

AGRPGNF.

Enzyme and pathway databases

BioCyc

HINF71421:HI_0607-MON.

Family and domain databases

HAMAP

MF_00222. Divergent sequence.
[Tree]

InterPro

IPR016040. NAD(P)-bd_dom.
IPR013708. Shikimate_DH-bd_N.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Y607_HAEIN

Accession

Primary (citable) accession number: P44774

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)