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Q9JYH8

- HISX_NEIMB

UniProt

Q9JYH8 - HISX_NEIMB

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
Reviewed - 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

Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301NADUniRule annotation
Binding sitei191 – 1911NADUniRule annotation
Binding sitei214 – 2141NADUniRule annotation
Binding sitei237 – 2371SubstrateUniRule annotation
Metal bindingi259 – 2591ZincUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Metal bindingi262 – 2621ZincUniRule annotation
Binding sitei262 – 2621SubstrateUniRule annotation
Active sitei327 – 3271Proton acceptorUniRule annotation
Active sitei328 – 3281Proton acceptorUniRule annotation
Binding sitei328 – 3281SubstrateUniRule annotation
Metal bindingi361 – 3611ZincUniRule annotation
Binding sitei361 – 3611SubstrateUniRule annotation
Binding sitei415 – 4151SubstrateUniRule annotation
Metal bindingi420 – 4201ZincUniRule annotation
Binding sitei420 – 4201SubstrateUniRule 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

BioCyciNMEN122586:GHGG-1623-MONOMER.
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:NMB1581
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000425: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Histidinol dehydrogenasePRO_0000135802Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi122586.NMB1581.

Structurei

3D structure databases

ProteinModelPortaliQ9JYH8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiYAAKLCG.
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.

Q9JYH8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKLNTQSPD FQAGLKALLA FETAQNPETE RIVADICADV QKRGDAALIE
60 70 80 90 100
YTNKFDQTNA KSIDDLILTQ ADLNAAFERI PNDVQTALQT AARRVESYHQ
110 120 130 140 150
RQKMESWSYT DEDGTLLGQQ ITPLDRVGIY VPGGKAAYPS SVIMNAMPAH
160 170 180 190 200
VAGVKEIIMV VPTPKGERND IVLAAAYVAG VTKVFTVGGA QAVAALAYGT
210 220 230 240 250
ETIPQVDKIT GPGNAFVAAA KRRVFGVVGI DMVAGPSEIL VIADGTTPAD
260 270 280 290 300
WVAMDLFSQA EHDEIAQAIL IGTSQAYLDE VEAAMDRLIE TMPRRDIIEA
310 320 330 340 350
SLGNRGAMIL AKDLDEACEI ANYISPEHLE LSVENPQEWA KKIRHAGAIF
360 370 380 390 400
MGRYTGESLG DYCAGPNHVL PTSRTARFSS PLGTYDFQKR SSLIQVSEQG
410 420
AQKLGETASV LAHGESLTAH ARAAEFRMK
Length:429
Mass (Da):46,324
Last modified:October 1, 2000 - v1
Checksum:i1A6597DF1E685847
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002098 Genomic DNA. Translation: AAF41934.1.
PIRiE81067.
RefSeqiNP_274587.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF41934; AAF41934; NMB1581.
GeneIDi904220.
KEGGinme:NMB1581.
PATRICi20359028. VBINeiMen85645_2032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002098 Genomic DNA. Translation: AAF41934.1 .
PIRi E81067.
RefSeqi NP_274587.1. NC_003112.2.

3D structure databases

ProteinModelPortali Q9JYH8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 122586.NMB1581.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF41934 ; AAF41934 ; NMB1581 .
GeneIDi 904220.
KEGGi nme:NMB1581.
PATRICi 20359028. VBINeiMen85645_2032.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
KOi K00013.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci NMEN122586:GHGG-1623-MONOMER.

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view ]
Pfami PF00815. Histidinol_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC58.

Entry informationi

Entry nameiHISX_NEIMB
AccessioniPrimary (citable) accession number: Q9JYH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: October 1, 2014
This is version 89 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