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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
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: L-histidine biosynthesis

This protein is involved in step 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisIE)
  3. Histidine biosynthesis bifunctional protein HisIE (hisIE)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei130NADUniRule annotation1
Binding sitei192NADUniRule annotation1
Binding sitei215NADUniRule annotation1
Binding sitei238SubstrateUniRule annotation1
Metal bindingi260ZincUniRule annotation1
Binding sitei260SubstrateUniRule annotation1
Metal bindingi263ZincUniRule annotation1
Binding sitei263SubstrateUniRule annotation1
Active sitei328Proton acceptorUniRule annotation1
Active sitei329Proton acceptorUniRule annotation1
Binding sitei329SubstrateUniRule annotation1
Metal bindingi362ZincUniRule annotation1
Binding sitei362SubstrateUniRule annotation1
Binding sitei416SubstrateUniRule annotation1
Metal bindingi421ZincUniRule annotation1
Binding sitei421SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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:syc2504_c
OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Taxonomic identifieri269084 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358631 – 434Histidinol dehydrogenaseAdd BLAST434

Interactioni

Protein-protein interaction databases

STRINGi269084.syc2504_c.

Structurei

3D structure databases

ProteinModelPortaliQ5MZ26.
SMRiQ5MZ26.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
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.

Q5MZ26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRIVSHLAE AQAELERICD RTHDDAVVHR EASVREIVQA VQRRGDAALI
60 70 80 90 100
EFTQEFDGFA LQAENLRVSG AELDAAYQQI PKELLDAIRL AHHQIEAFHR
110 120 130 140 150
QRVPKSWVQF GADGEVLGKR YTPVDRAGLY VPGGRAAYPS TVLMNAVPAK
160 170 180 190 200
VAGVERVVIT TPPGPDGSLN PAVLVAAQEA GIEEIYRVGG AQAIAALAYG
210 220 230 240 250
TATIPKVDVI SGPGNIYVTL AKKLVYGTVG IDSLAGPSEV LIIADRSANP
260 270 280 290 300
RWVAADLLAQ AEHDPLAAAI LITPDLELAT QVGFEVERQL QDHPRRLVTE
310 320 330 340 350
KAIAHYGLAI VVDSLETAVK LSNQFAPEHL ELEVEDPWAL VEQVRHAGAI
360 370 380 390 400
FLGSLTPEAI GDYVAGPNHT LPTSGAARYA SALSVETFLK SSSLIEYTAA
410 420 430
SLQRVARAVD VLATAEGLES HAESVRLRQQ SLDR
Length:434
Mass (Da):46,652
Last modified:February 1, 2005 - v1
Checksum:iF9880888CAC2B8B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD80694.1.
RefSeqiWP_011244814.1. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD80694; BAD80694; syc2504_c.
KEGGisyc:syc2504_c.
PATRICi32491234. VBISynElo117686_2846.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD80694.1.
RefSeqiWP_011244814.1. NC_006576.1.

3D structure databases

ProteinModelPortaliQ5MZ26.
SMRiQ5MZ26.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269084.syc2504_c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD80694; BAD80694; syc2504_c.
KEGGisyc:syc2504_c.
PATRICi32491234. VBISynElo117686_2846.

Phylogenomic databases

eggNOGiCOG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
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...

Entry informationi

Entry nameiHISX_SYNP6
AccessioniPrimary (citable) accession number: Q5MZ26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 1, 2005
Last modified: November 2, 2016
This is version 82 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

Documents

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

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 one 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.