ID A0A1J4UGE1_9BACT Unreviewed; 818 AA.
AC A0A1J4UGE1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Bifunctional aspartate kinase/homoserine dehydrogenase I {ECO:0000313|EMBL:OIO21526.1};
GN ORFNames=AUJ54_04465 {ECO:0000313|EMBL:OIO21526.1};
OS Ignavibacteria bacterium CG1_02_37_35.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1805220 {ECO:0000313|EMBL:OIO21526.1, ECO:0000313|Proteomes:UP000182308};
RN [1] {ECO:0000313|EMBL:OIO21526.1, ECO:0000313|Proteomes:UP000182308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_37_35 {ECO:0000313|EMBL:OIO21526.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO21526.1}.
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DR EMBL; MNVA01000050; OIO21526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4UGE1; -.
DR STRING; 1805220.AUJ54_04465; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000182308; 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 Gene3D; 3.30.70.260; -; 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:SF59; 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:OIO21526.1};
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 319..394
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 400..473
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 818 AA; 90015 MW; 52F96F2E125527A6 CRC64;
MKLLKFGGSS IASAERIKNV IEIIKSSLKK DKELAVVFSA YHSVTDKLVA ASHLAAEGNA
NYLDNLKELE NRHLAIAKEL ISVSKQSSAL ANIKFQLNEL DDILHGVFLI KELSLKTLDY
ILSFGERLSA YTISEILNDK KIANNFLDAR SVIKTDAQFG NARVLFDLTN KNIQKYFAAN
KKLQIVTGYI ASTIENETTT LGRGGSDFTA SIIGAALNAK EIEIWTDVDG VLTANPQKVK
NAFPIKHLTF NEAMELSHFG AKVIYPPTMQ PAHAKGIPLR IKNTFNPSAE GTLISKKKIA
NDFLIKGISS IDAISLVLVE GSGMVGVAGI AERIFSALAK KQINVILITQ ASSEHSICLA
IPPRDKKKAK EAIEFEFKLE LIEKKISEVK VENDFAIIAI VGENMQKTPG IAGRVFQALG
RNGINIAAIA QGSSELNISV VISKKDEAKA LNALHEAFFL SKTKSLHLFL VGPGLIGKTF
LTQLKNHQQK LAKEFSTSVH VCGIVNTKKM ILRKEGISLD KWEKELTSSN EISNLQTFVT
TLKEFNLRNS IFIDCTASEE VVNYYLDVLS SNISVVTPNK RANTKSFTFY KKLRETASKH
NVKFLYETNV GASLPIIGTI KDLVTSGDSM TKIEGILSGT LSYIFNSFKA GKKFSSVVLE
AREKGYTEPD PREDLNGKDV ARKLLILARE CGYQMELSDI KVENLIFPKA QKVKTVKEFF
GVLKENDGAF EKLRLKEEKD GKVLRYIAKL EKGKAEVSLQ AIDRTHPFFF MSGNDNILAV
HTLNYVHSPL VIKGPGAGAD VTAAGVFADV LRISNYLS
//
