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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Xylella fastidiosa (strain 9a5c)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.UniRule annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271NADUniRule annotation
Binding sitei189 – 1891NADUniRule annotation
Binding sitei212 – 2121NADUniRule annotation
Binding sitei237 – 2371SubstrateUniRule annotation
Metal bindingi259 – 2591ZincUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Metal bindingi262 – 2621ZincUniRule annotation
Binding sitei262 – 2621SubstrateUniRule annotation
Active sitei326 – 3261Proton acceptorUniRule annotation
Active sitei327 – 3271Proton acceptorUniRule annotation
Binding sitei327 – 3271SubstrateUniRule annotation
Metal bindingi360 – 3601ZincUniRule annotation
Binding sitei360 – 3601SubstrateUniRule annotation
Binding sitei414 – 4141SubstrateUniRule annotation
Metal bindingi419 – 4191ZincUniRule annotation
Binding sitei419 – 4191SubstrateUniRule annotation

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: UniProtKB-HAMAP
  2. NAD binding Source: InterPro
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:XF_2219
OrganismiXylella fastidiosa (strain 9a5c)
Taxonomic identifieri160492 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
ProteomesiUP000000812: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Histidinol dehydrogenasePRO_0000135885Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi160492.XF2219.

Structurei

3D structure databases

ProteinModelPortaliQ9PBC5.
SMRiQ9PBC5. Positions 2-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9PBC5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIIDWNQLD TAAQAQTLTR PAQTIATQTR EAVAALIEQV RRGGDTALRD
60 70 80 90 100
ITARLDGVDL ATFEVTAAEL AAAATAVAPE LQHAMQTAAA RIEAFHRAGM
110 120 130 140 150
TNGYRVETAP GVVCERLVRP IARVGLYVPA GSAPLFSTAL MLGVPARLAG
160 170 180 190 200
CREVVLCTPP SKDGRANPAV LLAARLTGVT RVFTLGGAQA IAAMAYGTAS
210 220 230 240 250
VPTCDKVFGP GNSFVTEAKQ QLAQAGVVAI DMPAGPSEVL VIADAAANPA
260 270 280 290 300
FIAADLLSQA EHGPDSQVLL LSDSDALMTA VQTALALQLQ QLSRAEIARQ
310 320 330 340 350
ALAQSRLIKV ATLETAFDIS NRYAPEHLIL ALRQPRAWLH RVAAAGSVFL
360 370 380 390 400
GDYTPEALGD YCSGTNHVLP TGGAARAYSG VSVSSFQNMI SVQAASRSGI
410 420 430
AEIGDCALTL ARAEGLDAHA NAVALRMGTV P
Length:431
Mass (Da):44,761
Last modified:October 1, 2000 - v1
Checksum:iE2F6E714417279CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003849 Genomic DNA. Translation: AAF85018.1.
PIRiF82585.
RefSeqiNP_299498.1. NC_002488.3.

Genome annotation databases

EnsemblBacteriaiAAF85018; AAF85018; XF_2219.
GeneIDi1127772.
KEGGixfa:XF2219.
PATRICi24134682. VBIXylFas578_2361.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003849 Genomic DNA. Translation: AAF85018.1.
PIRiF82585.
RefSeqiNP_299498.1. NC_002488.3.

3D structure databases

ProteinModelPortaliQ9PBC5.
SMRiQ9PBC5. Positions 2-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160492.XF2219.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF85018; AAF85018; XF_2219.
GeneIDi1127772.
KEGGixfa:XF2219.
PATRICi24134682. VBIXylFas578_2361.

Phylogenomic databases

eggNOGiCOG0141.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the plant pathogen Xylella fastidiosa."
    Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A.
    , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
    Nature 406:151-159(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 9a5c.

Entry informationi

Entry nameiHISX_XYLFA
AccessioniPrimary (citable) accession number: Q9PBC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.