Skip Header

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

Q6A8L5

- HISX_PROAC

UniProt

Q6A8L5 - HISX_PROAC

(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
Propionibacterium acnes (strain KPA171202 / DSM 16379)
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

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291NADUniRule annotation
Binding sitei193 – 1931NADUniRule annotation
Binding sitei222 – 2221NADUniRule annotation
Binding sitei245 – 2451SubstrateUniRule annotation
Metal bindingi267 – 2671ZincUniRule annotation
Binding sitei267 – 2671SubstrateUniRule annotation
Metal bindingi270 – 2701ZincUniRule annotation
Binding sitei270 – 2701SubstrateUniRule annotation
Active sitei336 – 3361Proton acceptorUniRule annotation
Active sitei337 – 3371Proton acceptorUniRule annotation
Binding sitei337 – 3371SubstrateUniRule annotation
Metal bindingi370 – 3701ZincUniRule annotation
Binding sitei370 – 3701SubstrateUniRule annotation
Binding sitei424 – 4241SubstrateUniRule annotation
Metal bindingi429 – 4291ZincUniRule annotation
Binding sitei429 – 4291SubstrateUniRule 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

BioCyciPACN267747:GHO9-1165-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:PPA1152
OrganismiPropionibacterium acnes (strain KPA171202 / DSM 16379)
Taxonomic identifieri267747 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium
ProteomesiUP000000603: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Histidinol dehydrogenasePRO_0000135817Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi267747.PPA1152.

Structurei

3D structure databases

ProteinModelPortaliQ6A8L5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiQKSLHAV.
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.

Q6A8L5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRIVDVTSE TTDDLRCAVP RADFDVDAAM AAVIPVCSAV RDRGVEALRE
60 70 80 90 100
YSEKFDHVVP EHLRVPVEAL ATAAANLDGT LRRAFSESIR RRRQVCQEAE
110 120 130 140 150
VETSSQPVEV AGGARVSQRI VPVGRVGLYV PGGFAPLASS VIMNVVPAQE
160 170 180 190 200
AGVSSIAVAS PPQAEFGGLP HPSILALCHL LGVNEVYAVG GAQAIAMFAY
210 220 230 240 250
GVEGSDEADS CPRVDMVTGP GNIYVVAAKR CLRGTVGIDS EAGPTEIAIL
260 270 280 290 300
ADETADPRHI AADLMSQAEH DTLAAAVLVT DSTTLAEAVQ RELAPMVSAT
310 320 330 340 350
LHSERIRTSL TSKQSAIVMV RDIDQGLEVV NAYAAEHLEI QTADAAAVAA
360 370 380 390 400
RVWNAGAIFV GPWAPVSLGD YSAGSTHVLP TAGAACHSSG LSVRSFMRAV
410 420 430
HVIDYTEDAL LELADSVEAF ALAENLPGHA NAITVRRSR
Length:439
Mass (Da):46,098
Last modified:September 13, 2004 - v1
Checksum:iF1B7C0C567681677
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017283 Genomic DNA. Translation: AAT82901.1.
RefSeqiYP_055859.1. NC_006085.1.

Genome annotation databases

EnsemblBacteriaiAAT82901; AAT82901; PPA1152.
GeneIDi2932004.
KEGGipac:PPA1152.
PATRICi23037039. VBIProAcn64440_1188.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017283 Genomic DNA. Translation: AAT82901.1 .
RefSeqi YP_055859.1. NC_006085.1.

3D structure databases

ProteinModelPortali Q6A8L5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 267747.PPA1152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT82901 ; AAT82901 ; PPA1152 .
GeneIDi 2932004.
KEGGi pac:PPA1152.
PATRICi 23037039. VBIProAcn64440_1188.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci PACN267747:GHO9-1165-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 Propionibacterium acnes, a commensal of human skin."
    Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
    Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KPA171202 / DSM 16379.

Entry informationi

Entry nameiHISX_PROAC
AccessioniPrimary (citable) accession number: Q6A8L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: September 13, 2004
Last modified: November 26, 2014
This is version 78 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