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Protein

Bifunctional aspartokinase/homoserine dehydrogenase

Gene

thrA

Organism
Yersinia pestis
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + L-aspartate = ADP + 4-phospho-L-aspartate.UniRule annotation
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.UniRule annotation

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 1 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Aspartokinase (AU253_09460), Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Aspartokinase (lysC2), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Aspartokinase (apk), Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
  2. Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd)
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA), 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
  4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB), 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 and 3 of the subpathway that synthesizes L-homoserine from L-aspartate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Aspartokinase (AU253_09460), Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Aspartokinase (lysC2), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Aspartokinase (apk), Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
  2. Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd)
  3. Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Pathwayi: L-threonine biosynthesis

This protein is involved in step 1 and 3 of the subpathway that synthesizes L-threonine from L-aspartate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Aspartokinase (AU253_09460), Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Aspartokinase (lysC2), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Aspartokinase (apk), Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
  2. Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd)
  3. Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (metL), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
  4. Homoserine kinase (thrB), Homoserine kinase (thrB)
  5. no protein annotated in this organism
This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinaseUniRule annotationImported, OxidoreductaseUniRule annotation, Transferase
Biological processAmino-acid biosynthesisUniRule annotation
LigandATP-bindingUniRule annotation, NADPUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00034; UER00015.
UPA00050; UER00063.
UPA00050; UER00461.
UPA00051; UER00462.
UPA00051; UER00465.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional aspartokinase/homoserine dehydrogenaseUniRule annotation
Including the following 2 domains:
AspartokinaseUniRule annotation (EC:2.7.2.4UniRule annotation)
Homoserine dehydrogenaseUniRule annotation (EC:1.1.1.3UniRule annotation)
Gene namesi
Name:thrAImported
Ordered Locus Names:YPO0459Imported
OrganismiYersinia pestisImported
Taxonomic identifieri632 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
Proteomesi
  • UP000000815 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Proteomic databases

PaxDbiQ0WJK7.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi187410.y3718.

Structurei

3D structure databases

ProteinModelPortaliQ0WJK7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini320 – 394ACTInterPro annotationAdd BLAST75
Domaini401 – 478ACTInterPro annotationAdd BLAST78

Sequence similaritiesi

In the C-terminal section; belongs to the homoserine dehydrogenase family.UniRule annotation
In the N-terminal section; belongs to the aspartokinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CFH. Bacteria.
COG0460. LUCA.
COG0527. LUCA.
HOGENOMiHOG000271593.
KOiK12524.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
InterProiView protein in InterPro
IPR036393. AceGlu_kinase-like_sf.
IPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005106. Asp/hSer_DH_NAD-bd.
IPR001341. Asp_kinase.
IPR018042. Aspartate_kinase_CS.
IPR011147. Bifunc_aspartokin/hSer_DH.
IPR027795. GATS-like_ACT_dom.
IPR001342. HDH_cat.
IPR019811. HDH_CS.
IPR036291. NAD(P)-bd_dom_sf.
PfamiView protein in Pfam
PF00696. AA_kinase. 1 hit.
PF01842. ACT. 1 hit.
PF13840. ACT_7. 1 hit.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
PIRSFiPIRSF000727. ThrA. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
PROSITEiView protein in PROSITE
PS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0WJK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLKFGGTS VANAERFMRV ADIIESNARQ GQVATVLSAP AKITNHLVAM
60 70 80 90 100
IDKMVAGQDI SPNISDAERI FAELLRGLAD TQPGFDYDRL KALVGHEFAQ
110 120 130 140 150
LKHLLHGISL LGQCPDSINA SIICRGEKLS IAIMEALFQA KGYHVTVINP
160 170 180 190 200
VEKLLAQGHY LESTVDITES TRRIGASGIP SDHIILMAGF TAGNDKGELV
210 220 230 240 250
VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRTV PDARLLKSMS
260 270 280 290 300
YQEAMELSYF GAKVLHPRTI APIARFQIPC LIKNTSNPQA PGTLIGGESI
310 320 330 340 350
DEDSPVKGIT NLNNMAMINV SGPGMKGMVG MAARVFAVMS RSGISVVLIT
360 370 380 390 400
QSSSEYSISF CVPQGELLRA RRALEDEFYL ELKDGVLDPL DVMEHLAIIS
410 420 430 440 450
VVGDGMRTLR GISARFFSAL ARANINIIAI AQGSSERSIS VVVNNDAVTT
460 470 480 490 500
GVRVCHQMLF NTDQVIEVFV IGVGGVGGAL IEQIYRQQPW LKQRHIDLRV
510 520 530 540 550
CGIANSKAML TNVHGIALDN WRQELAEVQE PFNLSRLIRL VKEYHLLNPV
560 570 580 590 600
IVDCTSSQAV ADQYADFLTD GFHVVTPNKK ANTSSMNYYR QMRAAATKSC
610 620 630 640 650
RKFLYDTNVG AGLPVIENLQ NLLNAGDELM RFTGILSGSL SFIFGKLDEG
660 670 680 690 700
MSLSEATRQA KALGYTEPDP RDDLSGMDVA RKLLILAREA GYKLELADIE
710 720 730 740 750
VESVLPASFD ASGDVDTFLA RLPSLDAEFT RLVANAAEQG KVLRYVGVIE
760 770 780 790 800
DGRCKVRMEA VDGNDPLYKV KNGENALAFY TRYYQPIPLV LRGYGAGNDV
810
TAAGVFADLL RTLSWKLGV
Length:819
Mass (Da):89,110
Last modified:September 5, 2006 - v1
Checksum:iE8249C805C945285
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL19138.1.
PIRiAH0056.
RefSeqiWP_002209237.1. NZ_PDBR01000043.1.
YP_002345531.1. NC_003143.1.

Genome annotation databases

GeneIDi1173303.
KEGGiype:YPO0459.
ypj:CH55_2348.
ypl:CH46_454.
ypv:BZ15_3111.
ypw:CH59_1401.
PATRICifig|214092.21.peg.705.

Similar proteinsi

Entry informationi

Entry nameiQ0WJK7_YERPE
AccessioniPrimary (citable) accession number: Q0WJK7
Entry historyiIntegrated into UniProtKB/TrEMBL: September 5, 2006
Last sequence update: September 5, 2006
Last modified: January 31, 2018
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported