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A9HFM4 (A9HFM4_GLUDA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceInferred 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. SAAS SAAS022695 PIRNR PIRNR000099 HAMAP-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. SAAS SAAS022695 PIRNR PIRNR000099 HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. SAAS SAAS022695 PIRSR PIRSR000099-4 HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. SAAS SAAS022695 PIRNR PIRNR000099 HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family. RuleBase RU004175 PIRNR PIRNR000099 HAMAP-Rule MF_01024

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site3261Proton acceptor By similarity PIRSR PIRSR000099-1 HAMAP-Rule MF_01024
Active site3271Proton acceptor By similarity PIRSR PIRSR000099-1 HAMAP-Rule MF_01024
Metal binding2581Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding2611Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding3601Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding4191Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Binding site1291NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024
Binding site1901NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024
Binding site2131NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024
Binding site2361Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2581Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2611Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3271Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3601Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site4141Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site4191Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Sequences

Sequence LengthMass (Da)Tools
A9HFM4 [UniParc].

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

FASTA43745,822
        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

[1]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.
Strain: PAl 5 EMBL ACI51898.1.
[2]"Complete genome sequence of the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5."
Bertalan M., Albano R., de 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. expand/collapse author list , Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O., Baldani J.I., Ferreira P.C.
BMC Genomics 10:450-450(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 49037 / DSM 5601 / PAl5 and PAl 5 EMBL CAP55383.1.
[3]"Two genome sequences of the same bacterial strain, Gluconacetobacter diazotrophicus PAl 5, suggest a new standard in genome sequence submission."
Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.
Stand. Genomic Sci. 2:309-317(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 49037 / DSM 5601 / PAl5 and PAl 5 EMBL ACI51898.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001189 Genomic DNA. Translation: ACI51898.1.
AM889285 Genomic DNA. Translation: CAP55383.1.
RefSeqYP_001601696.1. NC_010125.1.
YP_002276513.1. NC_011365.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272568.GDI_1440.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI51898; ACI51898; Gdia_2140.
CAP55383; CAP55383; GDI1440.
GeneID5791558.
6975568.
KEGGgdi:GDI_1440.
gdj:Gdia_2140.
PATRIC22052716. VBIGluDia203729_2139.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycGDIA272568:GJPS-1464-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA9HFM4_GLUDA
AccessionPrimary (citable) accession number: A9HFM4
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)