Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5F7D8

- HISX_NEIG1

UniProt

Q5F7D8 - HISX_NEIG1

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
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

BioCyciNGON242231:GI2G-1152-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:NGO1240
OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Taxonomic identifieri242231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000535: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Histidinol dehydrogenasePRO_0000135800Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi242231.NGO1240.

Structurei

3D structure databases

ProteinModelPortaliQ5F7D8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiCAIANRI.
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.

Q5F7D8-1 [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 QAIAALAYGT
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 VKDLNEACEI SNYISPEHLE LSVENPQEWA KKIRHAGAIF
360 370 380 390 400
MGRYTGESLG DYCAGPNHVL PTSRTARFSS PLGTYDFQKR SSLIQVSEQG
410 420
AQKLGETASV LAHGESLTAH ARAAEFRMK
Length:429
Mass (Da):46,381
Last modified:March 15, 2005 - v1
Checksum:i1308394D43951E17
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004969 Genomic DNA. Translation: AAW89899.1.
RefSeqiYP_208311.1. NC_002946.2.

Genome annotation databases

EnsemblBacteriaiAAW89899; AAW89899; NGO1240.
GeneIDi3282462.
KEGGingo:NGO1240.
PATRICi20335799. VBINeiGon24812_1459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004969 Genomic DNA. Translation: AAW89899.1 .
RefSeqi YP_208311.1. NC_002946.2.

3D structure databases

ProteinModelPortali Q5F7D8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 242231.NGO1240.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW89899 ; AAW89899 ; NGO1240 .
GeneIDi 3282462.
KEGGi ngo:NGO1240.
PATRICi 20335799. VBINeiGon24812_1459.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci NGON242231:GI2G-1152-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. "The complete genome sequence of Neisseria gonorrhoeae."
    Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
    , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700825 / FA 1090.

Entry informationi

Entry nameiHISX_NEIG1
AccessioniPrimary (citable) accession number: Q5F7D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 15, 2005
Last modified: October 1, 2014
This is version 70 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