Putative histidine biosynthesis bifunctional protein hisCD - Photorhabdus luminescens subsp. laumondii

Names and origin

Protein names

Recommended name:
    Putative histidine biosynthesis bifunctional protein hisCD
Including the following 2 domains:
    1- Recommended name:
            Histidinol dehydrogenase
                Short name=HDH
              EC=1.1.1.23
    2- Recommended name:
            Histidinol-phosphate aminotransferase
              EC=2.6.1.9
        Alternative name(s):
            Imidazole acetol-phosphate transaminase

Gene names

Name:	hisCD
Synonyms:	hisD
Ordered Locus Names:	plu1569

Organism

Photorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP]

Taxonomic identifier

141679 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus

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Protein attributes

Sequence length	807 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Function	Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity.
Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. L-histidinol + 2 NAD(+) = L-histidine + 2 NADH.
Cofactor	Binds 1 zinc ion per subunit By similarity. Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Subunit structure	Homodimer By similarity.
Sequence similarities	In the N-terminal section; belongs to the histidinol dehydrogenase family. In the C-terminal section; belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Metal-binding NAD Pyridoxal phosphate Zinc
Molecular function	Aminotransferase Oxidoreductase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: HAMAP histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 807

807

Putative histidine biosynthesis bifunctional protein hisCD

PRO_0000153415

Regions

Region

1 – 440

440

Histidinol dehydrogenase

Region

441 – 807

367

Histidinol-phosphate aminotransferase

Sites

Active site

328

1

By similarity

Active site

329

1

By similarity

Metal binding

261

1

Zinc By similarity

Metal binding

264

1

Zinc By similarity

Metal binding

362

1

Zinc By similarity

Metal binding

421

1

Zinc By similarity

Binding site

655

1

Pyridoxal phosphate (covalent) By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q7N6I1-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 648F98DD2F9F706E
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FASTA

807

88,850

        10         20         30         40         50         60 
MTDHFDTLIR WQECHDEQQN ALLTRPAISA SVEISRTVEQ ILHAVKEYGD HTLREFSRRF 

        70         80         90        100        110        120 
DKTVIENIRI SPEEIAAAEN SLNNDIKQAM QQAMNNIRVF HEAQKPIKIE VETQPGVYCQ 

       130        140        150        160        170        180 
QVTRPIDSVG LYIPGGSAPL LSTVLMLGTP AQIAGCHKVV LCSPPPIANE ILYAATLCGI 

       190        200        210        220        230        240 
TEIFQIGGAQ AIAAMAFGTE SVPKVDKIFG PGNAYVTEAK RQVSQRVDGA TIDMPAGPSE 

       250        260        270        280        290        300 
LLIIADAGAN PVFVAADLLS QAEHGPDSQV ILVTPDEALA KKVITEIEKQ LTRLPRNQIA 

       310        320        330        340        350        360 
AKALAHSRII VTTSLQQCVE ISNRYGPEHL IIQTRQPEQL VEKITSAGSV FLGDWSPESA 

       370        380        390        400        410        420 
GDYASGTNHV LPTYGYTSTY SSLGLADFLK RMTIQQLTPQ GLLNLSQTIE TLAQAEQLTA 

       430        440        450        460        470        480 
HKNALTLRVA ALNIAGQGVN MNNIFDANLL ARENIRKLTP YMSARRLGGK GDVWLNANEY 

       490        500        510        520        530        540 
PLAPDFQCTE QTLNRYPDCQ PASVIRRYAA YAGLQPEQVL ACRGADESIE LLIRVFCEPG 

       550        560        570        580        590        600 
QDVVLFCPPT YGMYSVSAET FGVEQKKITA LENWQLDIEA IENNLDRVKL IYICSPNNPT 

       610        620        630        640        650        660 
GNAINPDSLR KILELTANRA IVTIDEAYIE FCPENSIASW LKNYPNLVIL RTLSKAFALA 

       670        680        690        700        710        720 
GLRCGFTLAS VDIITLLLKV IAPYPLSTPV ADIAAQALTA ENIAIMQKRV VEIRENRNDL 

       730        740        750        760        770        780 
QQALNKLAIV EKVFPSETNY ILVKFYDAET VFKTLWHQGI ILRDQRKQPG LEGCLRITIG 

       790        800 
SRKECERVVE AISALSTVNE QPKEIAN

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References

[1]

"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens."
Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K.

Kunst F.
Nat. Biotechnol. 21:1307-1313(2003) [PubMed: 14528314] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TT01.

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Cross-references

Sequence databases
	BX571864 Genomic DNA. Translation: CAE13862.1.
RefSeq	NP_928860.1.
3D structure databases
SMR	Q7N6I1. Positions 5-432.
ModBase	Search...
Genome annotation databases
GeneID	2801564.
GenomeReviews	Gene locus plu1569 in contig BX470251_GR.
KEGG	plu:plu1569.
NMPDR	fig\|243265.1.peg.1484.
Organism-specific databases
PhotoList	plu1569.
CMR	Search...
Phylogenomic databases
HOGENOM	Q7N6I1.
Enzyme and pathway databases
BioCyc	PLUM243265:PLU1569-MON.
Family and domain databases
HAMAP	MF_01023. Fused. [Tree] MF_01024. Fused. [Tree]
InterPro	IPR004839. Aminotrans_I/II. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR005861. HisP_aminotrans. IPR001692. Histidinol_DHase. IPR012131. Hstdl_DHase_prok. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. PF00815. Histidinol_dh. 1 hit. [Graphical view]
PRINTS	PR00083. HOLDHDRGNASE.
ProDom	PD002680. Histidinol_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01141. hisC. 1 hit. TIGR00069. hisD. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HIS8_PHOLL

Accession

Primary (citable) accession number: Q7N6I1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	December 15, 2003
Last modified:	November 25, 2008
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents