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Q9PM77

- HISX_CAMJE

UniProt

Q9PM77 - HISX_CAMJE

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
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 sitei234 – 2341SubstrateUniRule annotation
Metal bindingi256 – 2561ZincUniRule annotation
Binding sitei256 – 2561SubstrateUniRule annotation
Metal bindingi259 – 2591ZincUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Active sitei323 – 3231Proton acceptorUniRule annotation
Active sitei324 – 3241Proton acceptorUniRule annotation
Binding sitei324 – 3241SubstrateUniRule annotation
Metal bindingi357 – 3571ZincUniRule annotation
Binding sitei357 – 3571SubstrateUniRule annotation
Binding sitei411 – 4111SubstrateUniRule annotation
Metal bindingi416 – 4161ZincUniRule annotation
Binding sitei416 – 4161SubstrateUniRule 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

BioCyciCJEJ192222:GJTS-1557-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:Cj1598
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000000799: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Histidinol dehydrogenasePRO_0000135751Add
BLAST

Proteomic databases

PRIDEiQ9PM77.

Interactioni

Protein-protein interaction databases

STRINGi192222.Cj1598.

Structurei

3D structure databases

ProteinModelPortaliQ9PM77.
SMRiQ9PM77. Positions 3-428.
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.

Q9PM77-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQILVYDNLD EKQKEEALKR PAISAKDEIS KIVSSIIKEV QEKGDKALIE
60 70 80 90 100
QALKFDKAEI SKIKITQEEI TQASNRLDKD LQEAILVAYE NIKKFHEAQI
110 120 130 140 150
PHEIALETTK GVKCEVLTRP IEKVGLYIPG GLAPLFSTVL MLAIPAKIAG
160 170 180 190 200
CEKIVLASPA KINDAVLFCA KLCGVDEIYQ MGGAGAIAAL TYGTQSVLKV
210 220 230 240 250
DKIFGPGNAF VTEAKRQVSS DINGAAIDMQ AGPSEVLVIA DDLANEKFVA
260 270 280 290 300
SDLLSQAEHG ADSQVILVCL SQDFAKKASD EVQSQLELLP RKELASKSIA
310 320 330 340 350
NSRIIIAKDL NQALEISNLY APEHLIIQTQ NPRELLKGVK HAGSVFLGAY
360 370 380 390 400
SPESMGDYAS GTNHVLPTYG LTKTHSSLGL ADFSKRMTVQ ELSKEGFLAL
410 420
GKSVEILAQN EHLDAHKNAV TFRLESLK
Length:428
Mass (Da):46,446
Last modified:October 1, 2000 - v1
Checksum:i16F08561BF7DB738
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35695.1.
PIRiD81255.
RefSeqiYP_002344967.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35695; CAL35695; Cj1598.
GeneIDi905868.
KEGGicje:Cj1598.
PATRICi20060156. VBICamJej33762_1574.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35695.1 .
PIRi D81255.
RefSeqi YP_002344967.1. NC_002163.1.

3D structure databases

ProteinModelPortali Q9PM77.
SMRi Q9PM77. Positions 3-428.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 192222.Cj1598.

Proteomic databases

PRIDEi Q9PM77.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL35695 ; CAL35695 ; Cj1598 .
GeneIDi 905868.
KEGGi cje:Cj1598.
PATRICi 20060156. VBICamJej33762_1574.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci CJEJ192222:GJTS-1557-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: NCTC 11168.

Entry informationi

Entry nameiHISX_CAMJE
AccessioniPrimary (citable) accession number: Q9PM77
Secondary accession number(s): Q0P830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: November 26, 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