ID Q8Z2Z6_SALTI Unreviewed; 810 AA.
AC Q8Z2Z6; A0A0C8UK14; Q7C6B3;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE Includes:
DE RecName: Full=Aspartokinase {ECO:0000256|PIRNR:PIRNR000727};
DE EC=2.7.2.4 {ECO:0000256|PIRNR:PIRNR000727};
DE Includes:
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR000727};
GN Name=metL {ECO:0000313|EMBL:CAD09522.1};
GN Synonyms=metM {ECO:0000313|EMBL:EBV0721241.1};
GN OrderedLocusNames=STY3768 {ECO:0000313|EMBL:CAD09522.1}, t3517
GN {ECO:0000313|EMBL:AAO71025.1};
GN ORFNames=CAJ76_11165 {ECO:0000313|EMBL:EDG8857419.1}, CAJ80_10130
GN {ECO:0000313|EMBL:EDG8901790.1}, CAJ85_13580
GN {ECO:0000313|EMBL:EDG8893435.1}, CAL67_05175
GN {ECO:0000313|EMBL:EDG8932120.1}, CB224_14350
GN {ECO:0000313|EMBL:EDH5801803.1}, CC884_09870
GN {ECO:0000313|EMBL:EDI0958092.1}, CC907_08715
GN {ECO:0000313|EMBL:EDI0993723.1}, CC972_14335
GN {ECO:0000313|EMBL:EDI1139796.1}, D4Z37_14020
GN {ECO:0000313|EMBL:EBS6526957.1}, D6Q30_10265
GN {ECO:0000313|EMBL:EBS1098701.1}, DKA88_14150
GN {ECO:0000313|EMBL:EBW2553640.1}, DNM71_13450
GN {ECO:0000313|EMBL:EBV0721241.1}, DNV09_07855
GN {ECO:0000313|EMBL:EBV1032621.1}, DS261_14440
GN {ECO:0000313|EMBL:EBX7034628.1}, DUQ91_15360
GN {ECO:0000313|EMBL:EBS0138189.1}, DUV11_14325
GN {ECO:0000313|EMBL:EBS5365183.1}, DVG36_12040
GN {ECO:0000313|EMBL:EBY2834374.1}, EBC38_12310
GN {ECO:0000313|EMBL:EBZ4082605.1}, EID90_10825
GN {ECO:0000313|EMBL:EBZ9855368.1}, ELQ62_10260
GN {ECO:0000313|EMBL:ECA4924331.1}, EU445_14170
GN {ECO:0000313|EMBL:ECB1385632.1}, EVI00_15095
GN {ECO:0000313|EMBL:ECB2194022.1}, F9R11_16125
GN {ECO:0000313|EMBL:EDB3137027.1}, F9Y21_14035
GN {ECO:0000313|EMBL:EDB3627256.1}, FI137_08330
GN {ECO:0000313|EMBL:EBG5393882.1}, G2227_13980
GN {ECO:0000313|EMBL:HAE0481948.1}, G2244_16190
GN {ECO:0000313|EMBL:HAE0418062.1}, G3982_001220
GN {ECO:0000313|EMBL:HAE3627674.1}, G3V49_003228
GN {ECO:0000313|EMBL:HAE1998165.1}, G4I71_002232
GN {ECO:0000313|EMBL:HAE6054970.1}, G4L28_004021
GN {ECO:0000313|EMBL:HAE6909276.1}, G4P30_002775
GN {ECO:0000313|EMBL:HAE7599346.1}, G4Y41_000539
GN {ECO:0000313|EMBL:HAE9014011.1}, G4Y55_003027
GN {ECO:0000313|EMBL:HAE9580185.1}, G9264_001886
GN {ECO:0000313|EMBL:HAF7398441.1}, G9C68_002988
GN {ECO:0000313|EMBL:HAF0687361.1}, G9X37_002250
GN {ECO:0000313|EMBL:HAF7361665.1}, GDI29_15050
GN {ECO:0000313|EMBL:EDH3996326.1}, GND71_003020
GN {ECO:0000313|EMBL:HAE7811118.1}, K3U68_17035
GN {ECO:0000313|EMBL:QZA28569.1}, ZZ17_08690
GN {ECO:0000313|EMBL:ECV8215786.1};
OS Salmonella typhi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370 {ECO:0000313|EMBL:CAD09522.1, ECO:0000313|Proteomes:UP000000541};
RN [1] {ECO:0000313|EMBL:CAD09522.1, ECO:0000313|Proteomes:UP000000541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18 {ECO:0000313|EMBL:CAD09522.1,
RC ECO:0000313|Proteomes:UP000000541};
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.,
RA Rutherford K., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2] {ECO:0000313|EMBL:AAO71025.1, ECO:0000313|Proteomes:UP000002670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2 {ECO:0000313|Proteomes:UP000002670}, and Ty2
RC {ECO:0000313|EMBL:AAO71025.1};
RX PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA Deng W., Liou S.R., Plunkett G.III., Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [3] {ECO:0000313|EMBL:HAE0418062.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=09-1703 {ECO:0000313|EMBL:HAE3627674.1}, 09-1978
RC {ECO:0000313|EMBL:HAE6054970.1}, 09-1979
RC {ECO:0000313|EMBL:HAE7599346.1}, 10-1436
RC {ECO:0000313|EMBL:HAE1998165.1}, 11-2088
RC {ECO:0000313|EMBL:HAE6909276.1}, 12-0098
RC {ECO:0000313|EMBL:HAF7398441.1}, 12-0437
RC {ECO:0000313|EMBL:HAF7361665.1}, 12-2005
RC {ECO:0000313|EMBL:HAE9014011.1}, 13-0747
RC {ECO:0000313|EMBL:HAF0687361.1}, 13-7562
RC {ECO:0000313|EMBL:HAE9580185.1}, IP E.88.374
RC {ECO:0000313|EMBL:HAE7811118.1},
RC Sam_1c96eabc-5ba9-4785-8bb4-b62bc64a6574
RC {ECO:0000313|EMBL:HAE0418062.1}, and
RC Sam_2e1fd039-ec06-4964-b74e-443d7665d7a0
RC {ECO:0000313|EMBL:HAE0481948.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [4] {ECO:0000313|EMBL:HAE1998165.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=09-1703 {ECO:0000313|EMBL:HAE3627674.1}, 09-1978
RC {ECO:0000313|EMBL:HAE6054970.1}, 09-1979
RC {ECO:0000313|EMBL:HAE7599346.1}, 10-1436
RC {ECO:0000313|EMBL:HAE1998165.1}, 11-2088
RC {ECO:0000313|EMBL:HAE6909276.1}, 12-0098
RC {ECO:0000313|EMBL:HAF7398441.1}, 12-0437
RC {ECO:0000313|EMBL:HAF7361665.1}, 12-2005
RC {ECO:0000313|EMBL:HAE9014011.1}, 13-0747
RC {ECO:0000313|EMBL:HAF0687361.1}, 13-7562
RC {ECO:0000313|EMBL:HAE9580185.1}, IP E.88.374
RC {ECO:0000313|EMBL:HAE7811118.1},
RC Sam_1c96eabc-5ba9-4785-8bb4-b62bc64a6574
RC {ECO:0000313|EMBL:HAE0418062.1}, and
RC Sam_2e1fd039-ec06-4964-b74e-443d7665d7a0
RC {ECO:0000313|EMBL:HAE0481948.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ECA4924331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=116585 {ECO:0000313|EMBL:EDG8932120.1}, 132015
RC {ECO:0000313|EMBL:EDG8901790.1}, 14549
RC {ECO:0000313|EMBL:ECV8215786.1}, 186520
RC {ECO:0000313|EMBL:EDG8893435.1}, 189261
RC {ECO:0000313|EMBL:EDG8857419.1}, 257355
RC {ECO:0000313|EMBL:EBW2553640.1}, 338438
RC {ECO:0000313|EMBL:EDI1139796.1}, 339489
RC {ECO:0000313|EMBL:EDI0958092.1}, 348081
RC {ECO:0000313|EMBL:EDI0993723.1}, 365365
RC {ECO:0000313|EMBL:EDH5801803.1}, 524805
RC {ECO:0000313|EMBL:EBY2834374.1}, 531284
RC {ECO:0000313|EMBL:EBV1032621.1}, 539099
RC {ECO:0000313|EMBL:EBV0721241.1}, 550116
RC {ECO:0000313|EMBL:EBX7034628.1}, 550675
RC {ECO:0000313|EMBL:ECB1385632.1}, 550679
RC {ECO:0000313|EMBL:EBS5365183.1}, 568336
RC {ECO:0000313|EMBL:EBS0138189.1}, 588927
RC {ECO:0000313|EMBL:EBS6526957.1}, 606246
RC {ECO:0000313|EMBL:EBS1098701.1}, 619925
RC {ECO:0000313|EMBL:EBZ4082605.1}, 643219
RC {ECO:0000313|EMBL:EBZ9855368.1}, 656788
RC {ECO:0000313|EMBL:ECA4924331.1}, 673629
RC {ECO:0000313|EMBL:ECB2194022.1}, 731618
RC {ECO:0000313|EMBL:EBG5393882.1}, 814947
RC {ECO:0000313|EMBL:EDB3137027.1}, 815592
RC {ECO:0000313|EMBL:EDB3627256.1}, and 824494
RC {ECO:0000313|EMBL:EDH3996326.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:QZA28569.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ISP2825 {ECO:0000313|EMBL:QZA28569.1};
RA Lee G.Y., Song J.;
RT "Complete Genome Sequence of Salmonella enterica Serovar Typhi Strain
RT ISP2825.";
RL Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000709,
CC ECO:0000256|PIRNR:PIRNR000727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001406};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000116,
CC ECO:0000256|PIRNR:PIRNR000727};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004766, ECO:0000256|PIRNR:PIRNR000727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004986, ECO:0000256|PIRNR:PIRNR000727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005062, ECO:0000256|PIRNR:PIRNR000727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139,
CC ECO:0000256|PIRNR:PIRNR000727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056,
CC ECO:0000256|PIRNR:PIRNR000727}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|PIRNR:PIRNR000727}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007952,
CC ECO:0000256|PIRNR:PIRNR000727}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase
CC family. {ECO:0000256|ARBA:ARBA00010046, ECO:0000256|PIRNR:PIRNR000727}.
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DR EMBL; AE014613; AAO71025.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD09522.1; -; Genomic_DNA.
DR EMBL; AAFJDY010000010; EBG5393882.1; -; Genomic_DNA.
DR EMBL; AAGUIA010000016; EBS0138189.1; -; Genomic_DNA.
DR EMBL; AAGULE010000016; EBS1098701.1; -; Genomic_DNA.
DR EMBL; AAGVVD010000015; EBS5365183.1; -; Genomic_DNA.
DR EMBL; AAGWES010000015; EBS6526957.1; -; Genomic_DNA.
DR EMBL; AAHEBT010000014; EBV0721241.1; -; Genomic_DNA.
DR EMBL; AAHEEH010000009; EBV1032621.1; -; Genomic_DNA.
DR EMBL; AAHHUX010000015; EBW2553640.1; -; Genomic_DNA.
DR EMBL; AAHLZU010000015; EBX7034628.1; -; Genomic_DNA.
DR EMBL; AAHNRO010000013; EBY2834374.1; -; Genomic_DNA.
DR EMBL; AAHRAJ010000013; EBZ4082605.1; -; Genomic_DNA.
DR EMBL; AAHSWZ010000013; EBZ9855368.1; -; Genomic_DNA.
DR EMBL; AAHUNO010000012; ECA4924331.1; -; Genomic_DNA.
DR EMBL; AAHWPO010000015; ECB1385632.1; -; Genomic_DNA.
DR EMBL; AAHWWI010000015; ECB2194022.1; -; Genomic_DNA.
DR EMBL; AAKUKE010000010; ECV8215786.1; -; Genomic_DNA.
DR EMBL; AALNBT010000016; EDB3137027.1; -; Genomic_DNA.
DR EMBL; AALNGB010000014; EDB3627256.1; -; Genomic_DNA.
DR EMBL; AAMFQS010000011; EDG8857419.1; -; Genomic_DNA.
DR EMBL; AAMFQZ010000015; EDG8893435.1; -; Genomic_DNA.
DR EMBL; AAMFRD010000014; EDG8901790.1; -; Genomic_DNA.
DR EMBL; AAMFRJ010000009; EDG8932120.1; -; Genomic_DNA.
DR EMBL; AAMHNJ010000015; EDH3996326.1; -; Genomic_DNA.
DR EMBL; AAMICL010000016; EDH5801803.1; -; Genomic_DNA.
DR EMBL; AAMJUX010000011; EDI0958092.1; -; Genomic_DNA.
DR EMBL; AAMJVG010000010; EDI0993723.1; -; Genomic_DNA.
DR EMBL; AAMJWL010000014; EDI1139796.1; -; Genomic_DNA.
DR EMBL; DAAQQG010000017; HAE0418062.1; -; Genomic_DNA.
DR EMBL; DAAQQU010000012; HAE0481948.1; -; Genomic_DNA.
DR EMBL; DAARDQ010000048; HAE1998165.1; -; Genomic_DNA.
DR EMBL; DAARRK010000008; HAE3627674.1; -; Genomic_DNA.
DR EMBL; DAASLV010000020; HAE6054970.1; -; Genomic_DNA.
DR EMBL; DAASSY010000051; HAE6909276.1; -; Genomic_DNA.
DR EMBL; DAASYX010000019; HAE7599346.1; -; Genomic_DNA.
DR EMBL; DAATAS010000016; HAE7811118.1; -; Genomic_DNA.
DR EMBL; DAATOU010000005; HAE9014011.1; -; Genomic_DNA.
DR EMBL; DAATPQ010000014; HAE9580185.1; -; Genomic_DNA.
DR EMBL; DAATYW010000015; HAF0687361.1; -; Genomic_DNA.
DR EMBL; DAAWCE010000043; HAF7361665.1; -; Genomic_DNA.
DR EMBL; DAAWDS010000016; HAF7398441.1; -; Genomic_DNA.
DR EMBL; CP080960; QZA28569.1; -; Genomic_DNA.
DR RefSeq; NP_457952.1; NC_003198.1.
DR RefSeq; WP_000110811.1; NZ_WSUR01000010.1.
DR AlphaFoldDB; Q8Z2Z6; -.
DR STRING; 220341.gene:17587633; -.
DR KEGG; stt:t3517; -.
DR KEGG; sty:STY3768; -.
DR PATRIC; fig|220341.7.peg.3844; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_7_2_6; -.
DR OMA; GAGVCKN; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04257; AAK_AK-HSDH; 1.
DR CDD; cd04892; ACT_AK-like_2; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 1.20.120.1320; Aspartokinase, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR049638; AK-HD.
DR InterPro; IPR041743; AK-HSDH_N.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR43070; -; 1.
DR PANTHER; PTHR43070:SF5; HOMOSERINE DEHYDROGENASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF000727; ThrA; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR000727};
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000727};
KW Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:EBG5393882.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000727};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000727};
KW Transferase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:EBS0138189.1}.
FT DOMAIN 12..284
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 465..599
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 608..803
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
SQ SEQUENCE 810 AA; 88875 MW; D823F45FE694D7E1 CRC64;
MSVIAQAGAK GRQLHKFGGS SLADVKCYLR VAGIMAEYSQ PDDMMVVSAA GSTTNQLISW
LKLSQTDRLS AHQVLQTLRR YQCDLISGLL PADAADDLTS AFISDLERLA ALLDGGVTDA
VYAEIVGHGE IWSARLMSAV LNQQGLDAAW LDARAFLRAE RAAQPQVDEG LSYPLLQQLL
AQHPGKRLVV TGFISRNHDG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP
RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSD IDLQLRCSYT PDQGSTRIER
VLASGTGARI VTSHDDICLI EFQVPASQDF RLAHKELDQI LKRAQARPLA VGVHRDRQLL
QFCYTAEVAD SVLKLLDDVG LPGELRLRQG LALVAMVGAG VTRNPLHCHR FWQQLKGQPV
EFTWQSEEGI SLVAVLRTGP TESLIQGLHQ SVFRAEKRIG LMLFGKGNIG SRWLELFARE
QSTLSARTGF EFVLAGVVDS RRSLLNYEGL DASRALAFFD DEAVEQDEES LFLWMRAHPY
DDLVVLDVTA SEQLADQYLD FASHGFHVIS ANKLAGASAS DKYRQIHDAF EKTGRYWLYN
ATVGAGLPIN HTVRDLIDSG DTILSISGIF SGTLSWLFLQ FDGTVPFTDL VDQAWQQGLT
EPDPRVDLSG KDVMRKLVIL AREAGYDIEP DQVRVESLVP AHCEEGSIDH FFENGDALNE
QMVQRLEAAR ELGLVLRYVA RFDANGKARV GVEAVRPEHP LAALLPCDNV FAIESRWYRD
NPLVIRGPGA GRDVTAGAIQ SDINRLAQLL
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