Putative histidine biosynthesis bifunctional protein hisCD - Photorhabdus luminescens subsp. laumondii (strain TT01)

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Q7N6I1 (HIS8_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Putative histidine biosynthesis bifunctional protein hisCD

Including the following 2 domains:

Histidinol dehydrogenase
Short name=HDH
EC=1.1.1.23
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 (strain TT01) [Complete proteome] [HAMAP]

Taxonomic identifier

243265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus

Protein attributes

Sequence length	807 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP MF_01023
Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023 L-histidinol + H₂O + 2 NAD⁺ = L-histidine + 2 NADH. HAMAP MF_01023
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01023 Pyridoxal phosphate By similarity. HAMAP MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023 Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Subunit structure	Homodimer By similarity. HAMAP MF_01023
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.

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: UniProtKB-KW
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 HAMAP MF_01023

PRO_0000153415

Regions

Region

1 – 440

440

Histidinol dehydrogenase HAMAP MF_01023

Region

441 – 807

367

Histidinol-phosphate aminotransferase HAMAP MF_01023

Sites

Active site

328

By similarity

Active site

329

By similarity

Metal binding

261

Zinc By similarity

Metal binding

264

Zinc By similarity

Metal binding

362

Zinc By similarity

Metal binding

421

Zinc By similarity

Amino acid modifications

Modified residue

655

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q7N6I1 [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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571864 Genomic DNA. Translation: CAE13862.1.
RefSeq	NP_928860.1. NC_005126.1.
3D structure databases
ProteinModelPortal	Q7N6I1.
SMR	Q7N6I1. Positions 5-432, 450-794.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2801564.
GenomeReviews	Gene locus plu1569 in contig BX470251_GR.
KEGG	plu:plu1569.
NMPDR	fig\|243265.1.peg.1484.
PATRIC	20507017. VBIPhoLum48522_1751.
Organism-specific databases
GenoList	plu1569.
CMR	Search...
Phylogenomic databases
PhylomeDB	Q7N6I1.
Enzyme and pathway databases
BioCyc	PLUM243265:PLU1569-MONOMER.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. Fused. [Tree] MF_01024. HisD. Fused. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR001692. Histidinol_DH_CS. IPR012131. Hstdl_DH. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00013.
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.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
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...

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:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents