Bifunctional aspartokinase/homoserine dehydrogenase - Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)

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Q89AR4 (AKH_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. 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:
Bifunctional aspartokinase/homoserine dehydrogenase
Short name=AK-HD

Including the following 2 domains:

Aspartokinase
EC=2.7.2.4
Homoserine dehydrogenase
EC=1.1.1.3

Gene names

Name:	thrA
Ordered Locus Names:	bbp_183

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	816 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-homoserine + NAD(P)⁺ = L-aspartate 4-semialdehyde + NAD(P)H. ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
Subunit structure	Homotetramer By similarity.
Sequence similarities	In the N-terminal section; belongs to the aspartokinase family. In the C-terminal section; belongs to the homoserine dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NADP binding Inferred from electronic annotation. Source: InterPro aspartate kinase activity Inferred from electronic annotation. Source: EC homoserine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 816

816

Bifunctional aspartokinase/homoserine dehydrogenase

PRO_0000066686

Regions

Nucleotide binding

472 – 479

NADP Potential

Region

1 – 250

250

Aspartokinase By similarity

Region

251 – 471

221

Interface By similarity

Region

472 – 816

345

Homoserine dehydrogenase By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q89AR4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: F8C3ADC0114576B5
Show »

FASTA

816

91,919

        10         20         30         40         50         60 
MKILKFGGTS LSNSELFFHV ATIIENNLNN EQIAIVLSAP GNTTNLLEIA INQTINNKNI 

        70         80         90        100        110        120 
IPIVQKIEKN FLKLINDIYQ VEQKLLYEKI KNNIENKLLE LKNLLQGINL LRQCPDKIRA 

       130        140        150        160        170        180 
KIISSGEYLS ISIMNSILIS RGYNTTIIDP VKKLLTKEDT YLNATVNIKI SKFRILSMKI 

       190        200        210        220        230        240 
PKHHIILMPG FTAGNKQGEL VTLGRNGSDY SATILSVCLN STMCEIWTDV NGVYTCDPKL 

       250        260        270        280        290        300 
VSDAKLLTSL SYREAIELSY LGAKILHPNT IYPIQKFKIP CTIKNTHNPS SIGTKISCNH 

       310        320        330        340        350        360 
VKNKNLITGV TYLENVHMFS ISCLYSKNIE TIIPKIFSCM SLSKIWIILT IQTSSQNTIS 

       370        380        390        400        410        420 
FCILKTMTNT ALHVLHKALY LELKHKLLKP IKVEKKLTLI SVISSDILNN TKITEKVFSI 

       430        440        450        460        470        480 
LKHVNINTLA ISKGASKNSI SIVVKHDDGI LGVRALHKGI FNKNCTAEIF LIGIGRVGQT 

       490        500        510        520        530        540 
FLKQIIEQKN WLKSKNIDLK ICGIANSKNF ILNLDGINPK NWKRDLNLSK KSFNFKHLLN 

       550        560        570        580        590        600 
SIQNYYLINP IIVDCTSDKN IANQYISFIN CGFHIVTPNK KANTTNWKYY EDIRLAAQKE 

       610        620        630        640        650        660 
KKKFFYETNV GAGLPVIENL KNLLRTGDTL IHFKGILSGS LSFIFGKLED NISLSEATKQ 

       670        680        690        700        710        720 
AQSLGFTEPN PKDDLSGIDV ARKLLILARE VGYKLELKDI KIEPLLPKEF NNISNTTDFI 

       730        740        750        760        770        780 
TKLKELDQIF CNRVKKARKL GKRLRFVGII NQKGNCQVKI DEVDHNDPLY NIKNGENALA 

       790        800        810 
FYSKYYQPIP LVLRGYGAGN NVTASGIFSD VLRILL

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References

[1]

"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO26915.1.
RefSeq	NP_777810.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89AR4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002587; EBBUCP00000002411; EBBUCG00000002587.
GeneID	1058230.
GenomeReviews	Gene locus bbp_183 in contig AE016826_GR.
KEGG	bab:bbp183.
PATRIC	21245141. VBIBucAph80364_0177.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000007710.
HOGENOM	HBG298754.
OMA	GANEMNI.
PhylomeDB	Q89AR4.
ProtClustDB	PRK09436.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_183-MONOMER.
Family and domain databases
InterPro	IPR001048. Asp/Glu/Uridylate_kinase. IPR005106. Asp/hSer_DH_NAD-bd. IPR001341. Asp_kinase_dom. IPR018042. Aspartate_kinase_CS. IPR011147. Bifunc_aspartokin/hSer_DH. IPR001342. HDH_cat. IPR019811. HDH_CS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 2 hits. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K12524.
Pfam	PF00696. AA_kinase. 1 hit. PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PIRSF	PIRSF000727. ThrA. 1 hit.
SUPFAM	SSF53633. Aa_kinase. 1 hit.
TIGRFAMs	TIGR00657. Asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. PS01042. HOMOSER_DHGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AKH_BUCBP

Accession

Primary (citable) accession number: Q89AR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 68 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

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