ID A0A267TKD6_9BACT Unreviewed; 818 AA.
AC A0A267TKD6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Bifunctional aspartate kinase/homoserine dehydrogenase I {ECO:0000313|EMBL:PAC33240.1};
GN ORFNames=BWI92_01655 {ECO:0000313|EMBL:PAC33240.1};
OS Flectobacillus sp. BAB-3569.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Flectobacillus.
OX NCBI_TaxID=1509483 {ECO:0000313|EMBL:PAC33240.1, ECO:0000313|Proteomes:UP000215844};
RN [1] {ECO:0000313|EMBL:PAC33240.1, ECO:0000313|Proteomes:UP000215844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-3569 {ECO:0000313|EMBL:PAC33240.1,
RC ECO:0000313|Proteomes:UP000215844};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Flectobacillus sp. BAB-3569 genome sequencing.";
RL Submitted (JUN-2017) 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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004766}.
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}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007952}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase
CC family. {ECO:0000256|ARBA:ARBA00010046}.
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:PAC33240.1}.
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DR EMBL; NJFZ01000003; PAC33240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267TKD6; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000215844; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04243; AAK_AK-HSDH-like; 1.
DR CDD; cd04921; ACT_AKi-HSDH-ThrA-like_1; 1.
DR CDD; cd04922; ACT_AKi-HSDH-ThrA_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 Gene3D; 3.30.2130.10; VC0802-like; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR049638; AK-HD.
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; IPR027795; CASTOR_ACT_dom.
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; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF13840; ACT_7; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF000727; ThrA; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
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; PS51671; ACT; 2.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Kinase {ECO:0000313|EMBL:PAC33240.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000215844};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:PAC33240.1}.
FT DOMAIN 319..397
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 400..471
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 818 AA; 89267 MW; 084C30C367D3A967 CRC64;
MKVLKFGGTS CGTVESIQSV LSIIKGNLVK GEKIAVVFSA MGGVTNQLIE TGKRAAVSDL
SYFDLVKTIE ERHFNVVRAL IDVKAQSKVF ANIRTIINEL EDLLKGVSLI REISSRTADL
IVSFGERLST TLIYEILHAQ GVDCQFLDAR KVIRTNDTFG MAEVDFDTTN SLIQEHFAKT
KSLQLITGFI GSTDKGETTT LGRGGSDYTG SIFGAALNSE EIEIWTDVDG MMTADPRKVK
NAFTIPTITY SEAMELTHFG AKVIYPPSLQ PAFARNIPIR VLNTFNPSFI GTVVSRQAEP
SEYIITGISS IDNLALVNLQ GSGMIGVAGV SGKLFTILAK HKISVVLISQ ASSEHSICFA
IDPQYSQEVR QILETEFASE IALGDIEGVD IQENLSVIAV VGEGMRHHTG VSGKLFSVLG
KNGINIVATA QGSSELNISV VIEKKDISKA LNVIHDTFFF SQVKTLNLFL VGTGLIGKAL
LNQLKGQANY LSKYRGLKVN LVGVMNSRKM LVTSDGISMD SWQETLDAMG KPAELWAFVE
EAKRLNLPNS VFADCTADKN IHNYYLGLFE SNISVVTPNK VANSGRYEDY ALLHRTVLKK
GVKFLYETNV GAGLPVINTL QGLIASGDRF EKIEGVLSGT LSYIFNNFKK GVKFADIVRE
AKVKGYTEPD PREDLSGMDV ARKILILGRE IGLRLEPEDV TILKLLPENC EKAPTVEDFF
NELEVSNSYF ETMVDEAEAK GEVLRFIATL EDNKITIGVK SIDKTHPFYM MDGADNVISF
TTKRYHDRPL VIKGPGAGAE VTASGVFADI VAIGSYLA
//
