NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sr41 / 8000, Sr41 / HNr21, Sr41 / HNr59, and Sr41 / TLr156;
PubMed=8423151 [NCBI, ExPASy, EBI, Israel, Japan]
Omori K., Suzuki S., Komatsubara S.;
"Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I.";
J. Bacteriol. 175:785-794(1993).

Comments

CATALYTIC ACTIVITY: L-homoserine + NAD(P)⁺ = L-aspartate 4-semialdehyde + NAD(P)H.
CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
ENZYME REGULATION: The enzyme activities are regulated allosterically by L-threonine.
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 1/4 .
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3 .
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3 .
PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5 .
PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5 .
SUBUNIT: Homotetramer.
SIMILARITY: In the N-terminal section; belongs to the aspartokinase family.
SIMILARITY: In the C-terminal section; belongs to the homoserine dehydrogenase family.
SIMILARITY: Contains 2 ACT domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D10385; BAA38474.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10386; BAA38477.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10387; BAA38480.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X60821; CAA43212.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B47057; B47057.

3D structure databases

HSSP

P31116; 1EBF. [HSSP ENTRY / PDB]

ModBase

P27725.

Family and domain databases

InterPro

IPR002912; ACT_bd.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR005106; Asp/hSer_DHase_NAD-bd.
IPR001341; Asp_kin_reg.
IPR011147; bifunc_aspartokin/hSer_DHase.
IPR001342; hSer_DHase_cat.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1160.10; Aa_kinase; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00696; AA_kinase; 1.
PF01842; ACT; 2.
PF00742; Homoserine_dh; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000727; ThrA; 1.

TIGRFAMs

TIGR00657; asp_kinases; 1.

PROSITE

PS00324; ASPARTOKINASE; 1.
PS01042; HOMOSER_DHGENASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allosteric enzyme; Amino-acid biosynthesis; Kinase; Multifunctional enzyme; NADP; Oxidoreductase; Repeat; Threonine biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 819`	`819`	`Bifunctional aspartokinase/homoserine dehydrogenase 1.`	`PRO_0000066682`
`DOMAIN`	`316 385`	`70`	`ACT 1.`
`DOMAIN`	`397 468`	`72`	`ACT 2.`
`NP_BIND`	`471 478`	`8`	`NADP (Potential).`
`REGION`	`1 249`	`249`	`Aspartokinase (By similarity).`
`REGION`	`250 470`	`221`	`Interface (By similarity).`
`REGION`	`471 819`	`349`	`Homoserine dehydrogenase (By similarity).`
`VARIANT`	`330 330`	`1`	`G -> D (in strain: Sr41 / 8000, Sr41 / HNr21; loss of feedback inhibition).`
`VARIANT`	`352 352`	`1`	`S -> F (in strain: Sr41 / TLr156; loss of feedback inhibition).`
`VARIANT`	`479 479`	`1`	`A -> T (in strain: Sr41 / HNr59; Thr-resistant HDI).`

Sequence information

Length: 819 AA [This is the length of the unprocessed precursor]

Molecular weight: 88495 Da [This is the MW of the unprocessed precursor]

CRC64: 1F18552B036A8E39 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVLKFGGTS VANAERFLRV ADIMESNARQ GQVATVLSAP AKITNHLVAM IDKTVAGQDI 

        70         80         90        100        110        120 
LPNMSDAERI FADLLSGLAQ ALPGFEYDRL KGVVDQEFAQ LKQVLHGVSL LGQCPDSVNA 

       130        140        150        160        170        180 
AIICRGEKLS IAIMEGVFRA KGYPVTVINP VEKLLAQGHY LESTVDIAES TLRIAAAAIP 

       190        200        210        220        230        240 
ADHIVLMAGF TAGNDKGELV VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRTV 

       250        260        270        280        290        300 
PDARLLKSMS YQEAMELSYF GAKVLHPRTI TPIAQFQIPC LIKNTSNPQA PGTLIGKDST 

       310        320        330        340        350        360 
DADMPVKGIT NLNNMAMINV SGPGMKGMVG MAARVFAVMS RAGISVVLIT QSSSEYSISF 

       370        380        390        400        410        420 
CVPQGELQRA RRALEEEFYL ELKDGVLDPL DVMERLAIIS VVGDGMRTLR GISARFFSAL 

       430        440        450        460        470        480 
ARANINIVAI AQGSSERSIS VVVSNDSATT GVRVSHQMLF NTDQVIEVFV IGVGGVGGAL 

       490        500        510        520        530        540 
IEQIYRQQPW LKQKHIDLRV CGIANSRVML TNVHGIALDS WRDALAGAQE PFNLGRLIRL 

       550        560        570        580        590        600 
VKEYHLLNPV IVDCTSSQAV ADQYVDFLAD GFHVVTPNKK ANTSSMNYYQ QLRAAAAGSH 

       610        620        630        640        650        660 
RKFLYDTNVG AGLPVIENLQ NLLNAGDELV RFSGILSGSL SFIFGKLDEG LSLSAATLQA 

       670        680        690        700        710        720 
RANGYTEPDP RDDLSGMDVA RKLLILAREA GYKLELSDIE VEPVLPPSFD ASGDVDTFLA 

       730        740        750        760        770        780 
RLPELDKEFA RNVANAAEQG KVLRYVGLID EGRCKVRIEA VDGNDPLYKV KNGENALAFY 

       790        800        810 
SRYYQPLPLV LRGYGAGNDV TAAGVFADLL RTLSWKLGV

P27725 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools