Reviewed, UniProtKB/Swiss-Prot Q8K9U9 (AKH_BUCAP)

Names and origin

Protein names

Recommended name:
    Bifunctional aspartokinase/homoserine dehydrogenase
      Short name=AK-HD
Including the following 2 domains:
    1- Recommended name:
            Aspartokinase
              EC=2.7.2.4
    2- Recommended name:
            Homoserine dehydrogenase
              EC=1.1.1.3

Gene names

Name:	thrA
Ordered Locus Names:	BUsg_188

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	814 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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; 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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NADP or NADPH 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 – 814	814	Bifunctional aspartokinase/homoserine dehydrogenase		PRO_0000066685
Regions
	Nucleotide binding	470 – 477	8	NADP Potential
	Region	1 – 248	248	Aspartokinase By similarity
	Region	249 – 469	221	Interface By similarity
	Region	470 – 814	345	Homoserine dehydrogenase By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9U9-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 162CDD52590D1A00	FASTA	814	91,379
	10 20 30 40 50 60 MKLLKFGGTS LANAKKFLCV ADIIEKKNKK EQIAVVLSAP AKITNYLATI IENKIDDEVL 70 80 90 100 110 120 KKINLAKNIF IELIQDIKRI QPLFPYENTK STIEIEFNKL KKIINGILLI KQCPEGIKPI 130 140 150 160 170 180 IISRGEILSV DIMKNILQSR NHEVTILNPV TNLLSIGNYL DSTIDIKESK KRIKKINIDQ 190 200 210 220 230 240 KNIILMAGFI AGNKEGELVV LGRNGSDYSA AILASCLNAK CCEIWTDVDG VLTADPRIVS 250 260 270 280 290 300 NTYLLDYISY QEAMELSYFG AKVLHPRTIE PISQFQIPCV IKNTNNTESK GTWIGKENNP 310 320 330 340 350 360 SDNSLKGVTY LDNIIMFNIS GSCLKDSGNT IARIFTILSR ESMKIILIIQ SSSENQINFC 370 380 390 400 410 420 TFEKDIDYIL LILKKEFTLE IKEGLLNDFN IVKNLTILSV IGSNISEKNN IASKIFSSLG 430 440 450 460 470 480 SSKINVLAIA HGSSKHSISI VIKKENLLQG IQNIHNTLFF KKTIINVFLI GIGGVGKALL 490 500 510 520 530 540 KQILKQEKFL DQKNIKIQFR MIANSKKLLF LKNSINLNNW EENFKKSKEK FNLTILNELL 550 560 570 580 590 600 KNTCDSNSVI IDCTSDYILS KQYISFIKKG FHIITSNKKA NTDSLKYYSE IRTTALKENK 610 620 630 640 650 660 KFLYETNVGA GLPVINTLQS LFSTGDCLIS FKGILSGSLS FIFGKLEEGV LLSEATKEAK 670 680 690 700 710 720 KLGFTEPNPF DDLSGIDVAR KLLVLAREIG YSIELKDISI EPILPERFKK YQNSEEFLFK 730 740 750 760 770 780 LKELDSFFSE RVNKARDIGN VLRFIGSIEK NGKCSVKIEE INSNNPLYKV KNGENALTFY 790 800 810 TNYYQPIPLV LRGYGAGNDV TASGVFSDLL RIIL

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013218 Genomic DNA. Translation: AAM67753.1.
RefSeq	NP_660542.1.
3D structure databases
HSSP	HSSP built from PDB template 1EBF based on UniProtKB P31116.
ModBase	Search...
Genome annotation databases
GeneID	1005385.
GenomeReviews	Gene locus BUsg_188 in contig AE013218_GR.
KEGG	bas:BUsg188.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8K9U9.
OMA	Q8K9U9. MFNVSGP.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG188-MON.
Family and domain databases
InterPro	IPR001048. Asp/Glu/Uridylate_kinase. IPR005106. Asp/hSer_DH_NAD-bd. IPR001341. Asp_kin_reg. IPR018042. Aspartate_kinase_CS. IPR011147. bifunc_aspartokin/hSer_DH. IPR001342. Homoserine_dehydrogenase_cat. IPR019811. Homoserine_dehydrogenase_CS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PIRSF	PIRSF000727. ThrA. 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_BUCAP

Accession

Primary (citable) accession number: Q8K9U9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 51 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)