Histidinol dehydrogenase - Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)

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A9HFM4 (A9HFM4_GLUDA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 51. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Histidinol dehydrogenase PIRNR PIRNR000099 HAMAP-Rule MF_01024
Short name=HDH PIRNR PIRNR000099 HAMAP-Rule MF_01024
EC=1.1.1.23 PIRNR PIRNR000099 HAMAP-Rule MF_01024

Gene names

Name:	hisD HAMAP-Rule MF_01024 EMBL CAP55383.1
Ordered Locus Names:	GDI1440 EMBL CAP55383.1, Gdia_2140 EMBL ACI51898.1

Organism

Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP] EMBL CAP55383.1

Taxonomic identifier

272568 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter ›

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. PIRNR PIRNR000099 HAMAP-Rule MF_01024 SAAS SAAS012131
Catalytic activity	L-histidinol + H₂O + 2 NAD⁺ = L-histidine + 2 NADH. PIRNR PIRNR000099 HAMAP-Rule MF_01024 SAAS SAAS012131
Cofactor	Binds 1 zinc ion per subunit By similarity. PIRSR PIRSR000099-4 HAMAP-Rule MF_01024 SAAS SAAS012131
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. PIRNR PIRNR000099 HAMAP-Rule MF_01024 SAAS SAAS012131
Sequence similarities	Belongs to the histidinol dehydrogenase family. RuleBase RU004175 PIRNR PIRNR000099 HAMAP-Rule MF_01024

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis PIRNR PIRNR000099 HAMAP-Rule MF_01024 SAAS SAAS012131
Ligand	Metal-binding PIRSR PIRSR000099-4 HAMAP-Rule MF_01024 SAAS SAAS012131 NAD PIRNR PIRNR000099 PIRSR PIRSR000099-2 HAMAP-Rule MF_01024 SAAS SAAS012131 Zinc PIRSR PIRSR000099-4 HAMAP-Rule MF_01024 SAAS SAAS012131
Molecular function	Oxidoreductase PIRNR PIRNR000099 HAMAP-Rule MF_01024 SAAS SAAS012131 EMBL ACI51898.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Active site

326

Proton acceptor By similarity PIRSR PIRSR000099-1 HAMAP-Rule MF_01024

Active site

327

Proton acceptor By similarity PIRSR PIRSR000099-1 HAMAP-Rule MF_01024

Metal binding

258

Zinc By similarity HAMAP-Rule MF_01024

Metal binding

261

Zinc By similarity HAMAP-Rule MF_01024

Metal binding

360

Zinc By similarity HAMAP-Rule MF_01024

Metal binding

419

Zinc By similarity HAMAP-Rule MF_01024

Binding site

129

NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024

Binding site

190

NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024

Binding site

213

NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024

Binding site

236

Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Binding site

258

Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Binding site

261

Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Binding site

327

Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Binding site

360

Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Binding site

414

Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Binding site

419

Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Sequences

Sequence

Length

Mass (Da)

Tools

A9HFM4 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 64E29B040A3D94A7
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FASTA

437

45,822

        10         20         30         40         50         60 
MKRLDTAQPD FRAAFARLLD DREGDTARVD APVAEILAAV RARGDEALCA YTARFDRMPV 

        70         80         90        100        110        120 
TPDRLRITEA EIEAACARVP PDLLAALDVA ATRIEAFHRA QMPADLRYTD ADGVDLGMRW 

       130        140        150        160        170        180 
TALDAVGLYV PGGTAAYPSS VLMNAMPARV AGAARLAMCV PTPDGVLNPL VLAAARRAGV 

       190        200        210        220        230        240 
TEIYRVGGAQ AVAAMAYGTA TIRPVDRVVG PGNAYVAEAK RQVFGRVGID SIAGPSEVVV 

       250        260        270        280        290        300 
VADSGTDPRI VALDLLAQAE HDALAQSILI TQDATLADRV AEAVEAELRT LPRAAIAGAS 

       310        320        330        340        350        360 
WGAHGAIITV RDLDEAASLI DAIAPEHLEL LLADPEPLFA RVRHAGAIFL GRQCAEAIGD 

       370        380        390        400        410        420 
YVGGPNHVLP TSRTARFASG LSVFDFLKRT TFIGAGPDAL RRIGPAAVAL ARAEGLDAHA 

       430 
LSVSARLDAV ARESDKA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gluconacetobacter diazotrophicus Pal5 complete genome." Bertalan M., Baldani I.J., Ferreira P. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49037 / DSM 5601 / PAl5.
[2]	"Complete sequence of chromosome of Gluconacetobacter diazotrophicus PAl 5." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Triplett E.W. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49037 / DSM 5601 / PAl5 and PAl 5 EMBL ACI51898.1.
[3]	"Complete genome sequence of the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5." Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A., Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D. Ferreira P.C. BMC Genomics 10:450-450(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: PAl 5 EMBL CAP55383.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001189 Genomic DNA. Translation: ACI51898.1. AM889285 Genomic DNA. Translation: CAP55383.1.
RefSeq	YP_001601696.1. NC_010125.1. YP_002276513.1. NC_011365.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	272568.GDI_1440.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACI51898; ACI51898; Gdia_2140. CAP55383; CAP55383; GDI1440.
GeneID	5791558. 6975568.
KEGG	gdi:GDI_1440. gdj:Gdia_2140.
PATRIC	22052716. VBIGluDia203729_2139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0141.
HOGENOM	HOG000243914.
KO	K00013.
OMA	PTYGYSR.
ProtClustDB	PRK00877.
Enzyme and pathway databases
BioCyc	GDIA272568:GJPS-1464-MONOMER.
UniPathway	UPA00031; UER00014.
Family and domain databases
HAMAP	MF_01024. HisD.
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR001692. Histidinol_DH_CS. IPR022695. Histidinol_DH_monofunct. IPR012131. Hstdl_DH. [Graphical view]
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000099. Histidinol_dh. 1 hit.
PRINTS	PR00083. HOLDHDRGNASE.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00069. hisD. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A9HFM4_GLUDA

Accession

Primary (citable) accession number: A9HFM4

Entry history

Integrated into UniProtKB/TrEMBL:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information