ID W6TYD9_9SPHI Unreviewed; 815 AA.
AC W6TYD9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Aspartokinase {ECO:0000313|EMBL:ETZ24303.1};
GN ORFNames=N824_14220 {ECO:0000313|EMBL:ETZ24303.1};
OS Pedobacter sp. V48.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ24303.1, ECO:0000313|Proteomes:UP000019145};
RN [1] {ECO:0000313|EMBL:ETZ24303.1, ECO:0000313|Proteomes:UP000019145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V48 {ECO:0000313|EMBL:ETZ24303.1,
RC ECO:0000313|Proteomes:UP000019145};
RX PubMed=24578271;
RA Bitzer A.S., Garbeva P., Silby M.W.;
RT "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT Coastal Sand Dune in the Netherlands.";
RL Genome Announc. 2:e00094-e00014(2014).
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:ETZ24303.1}.
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DR EMBL; AWRU01000003; ETZ24303.1; -; Genomic_DNA.
DR RefSeq; WP_048903647.1; NZ_AWRU01000003.1.
DR AlphaFoldDB; W6TYD9; -.
DR STRING; 509635.N824_14220; -.
DR PATRIC; fig|509635.5.peg.604; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000019145; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR018042; Aspartate_kinase_CS.
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; PS00324; ASPARTOKINASE; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETZ24303.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 318..390
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 399..477
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 815 AA; 89792 MW; BB358E9E5F9E270E CRC64;
MNILKFGGTS VGSVDSISAL IEILKPLQGE ENPIVVLSAM GGVTNALLDM AENARNLRDY
GDALKLVEEK HFKVIRTLLP AGAQNPVLTK LKIYFNELED ILQSVYNLRE LSAQTKDLIL
SYGERCSTIM ISHIAKQQFP NAVYVDGAEL IKTDSNFGQA KVNTYMTEML INDFYEANQD
KLLFVTGFIS SNDDGRVTTL GRGGSDYTAA IWGAALNASE IQIWTDVDGM LTADPRIVKK
AFSLPELSYT EAMELSYFGA KVIYPPTMIP AFLKKIPIVI KNTFNTAFAG TYIKHGISPS
NLPIKGISSI DEISVLNLSG SGMVGKAGFS GRLFSMLSRE QVNVVLITQS SSEHSITFAV
KPADSLKALS LINKEFELEL QARKLEYPEV ENGLSVVAIV GENMKRTPGM SGKLFSALGR
NGVNVRAIAQ GSSEYNISVI ISKTDLSKAV NAIHDAFYAD LKKTLHVFCL GTGNIGKTLF
KQLQDQMPFL ADNNDLQVKV MGVSNTRKMY LDPRGIDLNT WEEDLNNQDT KASLPDFIRR
MKAMNLPNCV FVDNTASHNP VEFYLDILQS SISVVTCNKI GNSADYEQYA AFKQAARTYG
VDFFYETNVG AGLPIIRTLK DLMLSGDKVA CIEAILSGTI SYIFNNYKDG VLFHEVVKEA
QEKGYTEPDP RDDLNGKDFM RKMLILARDA GYALEEKDIE LENMLPPSCM AAESVADFYK
ELKNNSAYFE NLKKQATQDN KVLRYIGKLE GGKVSINLQM VDENHPFYTL SGSDNIISFT
TNRYKDRPLV VKGPGAGAEV TAAGVFADII NVGKR
//
