Reviewed, UniProtKB/Swiss-Prot P06988 (HISX_ECOLI)

Names and origin

Protein names

Recommended name:
    Histidinol dehydrogenase
      Short name=HDH
    EC=1.1.1.23

Gene names

Name:	hisD
Ordered Locus Names:	b2020, JW2002

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. HAMAP MF_01024
Catalytic activity	L-histidinol + 2 NAD+ = L-histidine + 2 NADH. HAMAP MF_01024
Cofactor	Binds 1 zinc ion per subunit. HAMAP MF_01024
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP MF_01024
Subunit structure	Homodimer. HAMAP MF_01024
Sequence similarities	Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 434

433

Histidinol dehydrogenase HAMAP MF_01024

PRO_0000135770

Sites

Active site

326

1

Proton acceptor HAMAP MF_01024

Active site

327

1

Proton acceptor HAMAP MF_01024

Metal binding

259

1

Zinc HAMAP MF_01024

Metal binding

262

1

Zinc HAMAP MF_01024

Metal binding

360

1

Zinc HAMAP MF_01024

Metal binding

419

1

Zinc HAMAP MF_01024

Binding site

130

1

NAD HAMAP MF_01024

Binding site

188

1

NAD HAMAP MF_01024

Binding site

211

1

NAD HAMAP MF_01024

Binding site

237

1

Substrate HAMAP MF_01024

Binding site

259

1

Substrate HAMAP MF_01024

Binding site

262

1

Substrate HAMAP MF_01024

Binding site

327

1

Substrate HAMAP MF_01024

Binding site

360

1

Substrate HAMAP MF_01024

Binding site

414

1

Substrate HAMAP MF_01024

Binding site

419

1

Substrate HAMAP MF_01024

Experimental info

Sequence conflict

15

1

E → V Ref.1

Sequence conflict

15

1

E → V Ref.2

Sequence conflict

22

1

M → T in CAA27610. Ref.2

Sequence conflict

150

1

S → R Ref.1

Sequence conflict

150

1

S → R Ref.2

Sequence conflict

157

1

V → A in CAA36882. Ref.3

Sequence conflict

313

1

L → S Ref.1

Sequence conflict

313

1

L → S Ref.2

Sequence conflict

403

1

L → V Ref.1

Sequence conflict

403

1

L → V Ref.2

Secondary structure

1

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434

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Helix

9 – 11

3

Helix

14 – 20

7

Helix

30 – 56

27

Beta strand

57 – 59

3

Helix

70 – 79

10

Helix

82 – 100

19

Beta strand

107 – 112

6

Beta strand

115 – 123

9

Beta strand

125 – 130

6

Beta strand

134 – 136

3

Helix

139 – 152

14

Beta strand

155 – 161

7

Helix

167 – 175

9

Beta strand

180 – 183

4

Helix

186 – 195

10

Beta strand

198 – 200

3

Beta strand

204 – 207

4

Helix

212 – 223

12

Beta strand

229 – 231

3

Beta strand

238 – 243

6

Helix

249 – 260

12

Beta strand

267 – 273

7

Helix

275 – 290

16

Helix

296 – 302

7

Beta strand

306 – 309

4

Helix

313 – 323

11

Beta strand

326 – 332

7

Helix

335 – 338

4

Helix

339 – 341

3

Beta strand

346 – 351

6

Helix

356 – 361

6

Beta strand

363 – 365

3

Helix

374 – 376

3

Helix

383 – 386

4

Beta strand

387 – 395

9

Helix

397 – 413

17

Helix

417 – 433

17

Sequences

	Sequence		Length	Mass (Da)
	P06988-1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 4B4F2EA00C9BEA4E	FASTA	434	46,110
	10 20 30 40 50 60 MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA LREYSAKFDK 70 80 90 100 110 120 TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT AQKLPPVDVE TQPGVRCQQV 130 140 150 160 170 180 TRPVASVGLY IPGGSAPLFS TVLMLATPAS IAGCKKVVLC SPPPIADEIL YAAQLCGVQD 190 200 210 220 230 240 VFNVGGAQAI AALAFGTESV PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL 250 260 270 280 290 300 VIADSGATPD FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ 310 320 330 340 350 360 ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL GDWSPESAGD 370 380 390 400 410 420 YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF SALASTIETL AAAERLTAHK 430 NAVTLRVNAL KEQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons." Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B. J. Mol. Biol. 203:585-606(1988) [PubMed: 3062174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region." Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B. Mol. Gen. Genet. 203:382-388(1986) [PubMed: 3018428] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Nucleotide and amino acid polymorphism in the gene for L-histidinol dehydrogenase of Escherichia coli K12." Savic D.J., Jovanovic G., Kostic T. Nucleic Acids Res. 18:3634-3634(1990) [PubMed: 2194167] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3100 / ATCC 14948 / DSM 6302.
[4]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors." Bruni C.B., Musti A.M., Frunzio R., Blasi F. J. Bacteriol. 142:32-42(1980) [PubMed: 6246067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-319.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[9]	"Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase." Barbosa J.A.R.G., Sivaraman J., Li Y., Larocque R., Matte A., Schrag J.D., Cygler M. Proc. Natl. Acad. Sci. U.S.A. 99:1859-1864(2002) [PubMed: 11842181] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X13462 Genomic DNA. Translation: CAA31812.1.
X03972 Genomic DNA. Translation: CAA27610.1.
X52656 Genomic DNA. Translation: CAA36882.1.
U00096 Genomic DNA. Translation: AAC75081.1.
AP009048 Genomic DNA. Translation: BAA15851.1.
M10483 Genomic DNA. Translation: AAA23962.1.

PIR

DEECHT. C64967.

RefSeq

AP_002621.1.
NP_416524.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K75	X-ray	1.75	A/B	1-434	[»]
1KAE	X-ray	1.70	A/B	1-434	[»]
1KAH	X-ray	2.10	A/B	1-434	[»]
1KAR	X-ray	2.10	A/B	1-434	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P06988.

2DBase-Ecoli

P06988.

Genome annotation databases

GeneID

946531.

GenomeReviews

Gene locus JW2002 in contig AP009048_GR.
Gene locus b2020 in contig U00096_GR.

KEGG

ecj:JW2002.
eco:b2020.

Organism-specific databases

EchoBASE

EB0442.

EcoGene

EG10447. hisD.

CMR

Search...

Phylogenomic databases

HOGENOM

P06988.

OMA

P06988. LDAHKNA.

Enzyme and pathway databases

BioCyc

EcoCyc:HISTDEHYD-MON.
MetaCyc:HISTDEHYD-MON.

Family and domain databases

HAMAP

MF_01024.
[Tree]

InterPro

IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH_prok-type.
[Graphical view]

PANTHER

PTHR21256:SF2. Hstdl_DH_prok. 1 hit.

Pfam

PF00815. Histidinol_dh. 1 hit.
[Graphical view]

PRINTS

PR00083. HOLDHDRGNASE.

ProDom

PD002680. Histidinol_dh. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00069. hisD. 1 hit.

PROSITE

PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HISX_ECOLI

Accession

Primary (citable) accession number: P06988
Secondary accession number(s): O08506, P78076, Q47254

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 98 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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