Reviewed, UniProtKB/Swiss-Prot Q89AR4 (AKH_BUCBP)

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:	bbp_183

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [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	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 – 816	816	Bifunctional aspartokinase/homoserine dehydrogenase		PRO_0000066686
Regions
	Nucleotide binding	472 – 479	8	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)
	Q89AR4-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: F8C3ADC0114576B5	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

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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO26915.1.
RefSeq	NP_777810.1.
3D structure databases
SMR	Q89AR4. Positions 3-463, 467-815.
ModBase	Search...
Genome annotation databases
GeneID	1058230.
GenomeReviews	Gene locus bbp_183 in contig AE016826_GR.
KEGG	bab:bbp183.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG298754.
OMA	MFNVSGP.
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. 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_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:	February 9, 2010
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)