ID A0AAJ0ZD37_9ENTR Unreviewed; 810 AA. AC A0AAJ0ZD37; DT 24-JUL-2024, integrated into UniProtKB/TrEMBL. DT 24-JUL-2024, sequence version 1. DT 02-OCT-2024, entry version 2. 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 ORFNames=J0A64_20700 {ECO:0000313|EMBL:MBU3769016.1}; OS Enterobacter roggenkampii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=1812935 {ECO:0000313|EMBL:MBU3769016.1, ECO:0000313|Proteomes:UP000813349}; RN [1] {ECO:0000313|EMBL:MBU3769016.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BK34275 {ECO:0000313|EMBL:MBU3769016.1}; RX PubMed=34079986; DOI=10.1093/cid/ciab511; RA Klein S., Boutin S., Kocer K., Fiedler M.O., Storzinger D., Weigand M.A., RA Tan B., Richter D., Rupp C., Mieth M., Mehrabi A., Hackert T., RA Zimmermann S., Heeg K., Nurjadi D.; RT "Rapid Development of Cefiderocol Resistance in Carbapenem-resistant RT Enterobacter cloacae During Therapy Is Associated With Heterogeneous RT Mutations in the Catecholate Siderophore Receptor cirA."; RL Clin. Infect. Dis. 74:905-908(2022). CC -!- FUNCTION: Bifunctional aspartate kinase and homoserine dehydrogenase CC that catalyzes the first and the third steps toward the synthesis of CC lysine, methionine and threonine from aspartate. CC {ECO:0000256|ARBA:ARBA00044938}. 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:ARBA00044882}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23777; CC Evidence={ECO:0000256|ARBA:ARBA00044882}; 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:ARBA00044923}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15759; CC Evidence={ECO:0000256|ARBA:ARBA00044923}; 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:ARBA00044905}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15763; CC Evidence={ECO:0000256|ARBA:ARBA00044905}; CC -!- COFACTOR: CC Name=a metal cation; Xref=ChEBI:CHEBI:25213; CC Evidence={ECO:0000256|ARBA:ARBA00001920}; 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBU3769016.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JAFKCP010000018; MBU3769016.1; -; Genomic_DNA. DR Proteomes; UP000813349; Unassembled WGS sequence. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR CDD; cd04257; AAK_AK-HSDH; 1. DR CDD; cd04892; ACT_AK-like_2; 1. DR Gene3D; 3.30.70.260; -; 2. 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_Aspkin/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|PIRNR:PIRNR000727}; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:MBU3769016.1}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|PIRNR:PIRNR000727}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000727}; Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}; KW Transferase {ECO:0000256|PIRNR:PIRNR000727}. FT DOMAIN 12..284 FT /note="Aspartate/glutamate/uridylate kinase" FT /evidence="ECO:0000259|Pfam:PF00696" FT DOMAIN 465..600 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; 88587 MW; 6CD17EC237550184 CRC64; MSVIAQAGAK GRQLHKFGGS SLADVKCYLR VAGIMTEYSQ PGDMMVVSAA GSTTNQLISW LKLSQTDRLS AHQVQQSLRR YQSELIAGLL PADVADGLIG AFTHDLERLA ALLDSGITDA VYAEVVGHGE VWSARLMAAV LQHLGVDAAW LDARDFLRAE RAAQPQVDEG LSYPLLQQLL VQHPGKRIVV TGFISRSNAG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSD IDLQLRCSYT PDQGSTRIER VLASGTGARI VTSHDDICLI EFQVPAGQDF RLAHKEIDTI LKRAQVRPLA VGVHNDRQLL QFCYTAEVAD SALKILDEAG LPGELRLRQG LALVAMVGAG VTRNPLHCHR FWQQLKGQPV EFTWQSEEGI SLVAVLRKGP TESLIQGLHT SLFRAEKRIG LVLFGKGNIG SRWLELFARE QVTLSARTGF EFILAGVVDS RRSLLNYEGL DASRALAFFN DEAVEQDEES LFLWMRAHPY DDLVVLDVTA SEQLADQYLD FASHGFHVIS ANKLAGASST DKYRQIHDAF EKTGRHWLYN ATVGAGLPVN HTVRDLIESG DSILALSGIF SGTLSWLFLQ FDGTVPFTDL VDQAWQQGLT EPDPRVDLSG KDVMRKLVIL AREAGYDIEP DSVRVESLVP AGCEEGSVDH FFENGEELNE QMVQRLEAAN EMGLVLRYVA RFEANGKARV GVEAVRPEHP LAALLPCDNV FAIESRWYRD NPLVIRGPGA GRDVTAGAIQ SDINRLAKLL //