ID A0A369QNZ6_9BACT Unreviewed; 814 AA.
AC A0A369QNZ6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Aspartate kinase {ECO:0000313|EMBL:RDC65405.1};
DE EC=1.1.1.3 {ECO:0000313|EMBL:RDC65405.1};
DE EC=2.7.2.4 {ECO:0000313|EMBL:RDC65405.1};
GN Name=thrA {ECO:0000313|EMBL:RDC65405.1};
GN ORFNames=AHMF7616_04035 {ECO:0000313|EMBL:RDC65405.1};
OS Adhaeribacter pallidiroseus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Adhaeribacter.
OX NCBI_TaxID=2072847 {ECO:0000313|EMBL:RDC65405.1, ECO:0000313|Proteomes:UP000253919};
RN [1] {ECO:0000313|EMBL:RDC65405.1, ECO:0000313|Proteomes:UP000253919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF7616 {ECO:0000313|EMBL:RDC65405.1,
RC ECO:0000313|Proteomes:UP000253919};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Adhaeribacter sp. HMF7616 genome sequencing and assembly.";
RL Submitted (APR-2018) 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:RDC65405.1}.
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DR EMBL; QASA01000001; RDC65405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369QNZ6; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000253919; 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; 1.
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:RDC65405.1};
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 ECO:0000313|EMBL:RDC65405.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253919};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RDC65405.1}.
FT DOMAIN 399..477
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 814 AA; 88988 MW; ED6BFB1EB073987A CRC64;
MIVLKFGGSS VSTPENILKV LAVVKSHASV NELAVVVSAF GGVTDSLINT SRLAEKGDLA
YKEELKKLEE RHLTAVKELI HATRQSAIIA NVKFLLNELE DILQGVYLVK ELSLKTLDFV
SSFGERLSSY LIAEAFKENG VPAFAADYRQ LIITDRTYGN AKVKFEVTNA RVKQYLTNTN
ELPVIPGFVG TTEHGETTTL GRGGSDYTAA IVAAALDSAS LEIWTDVNGM MTADPRRVKN
AIPIEELSYE EALELSYFGA KIIYPPTIQP ALSKKIPIRL KNTFEPAAPG TLITQNPRQS
EAPVKGIASI ENIALLTISG SGMVGASGIA MRFFGALANQ KVNVILITQA SSEHSITVGI
NQRDATRAQL AIEQEFQLEI QAGIVDKVNI QNDLAILALV GLNMKNTPGI AGKLFSSLGR
NGINIIAIAQ GTSELNISCV IQKKDEEKAL NTIHEAFFLS DIKTLHLFVV GTGTVGATLL
KQIKNQAFNL YKTLAIDIKL IGLTNSKQAV FNEKGIPWAQ WEEIFEQKGQ ESNIEIFVER
MAELNLPNAI FVDCTANPDV AATYKFLLER SISIVTPNKI AASSNYHTYK ELKTLAAKRG
VKYLYETNVG AGLPIISTLT DLIRSGDTVH KIEGIFSGTM NYLFNTVSAD KKLSTVVQEA
MDLGYAEPDP RIDLSGKDVA RKIMILARET GDNLELEDVH IKPFLPANCL QDSPMDQFWQ
NLRSYEDTFE GQRAEVESQG KGYRLVASWE DGKARIELRE VDKSHPFYSV SGSDNIILFT
TERYKTQPLI VKGSGAGAEV TAAGVFADII RIAN
//
