ID A0A2Z4LTH6_9FLAO Unreviewed; 1128 AA.
AC A0A2Z4LTH6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Homoserine O-acetyltransferase {ECO:0000313|EMBL:AWX45235.1};
DE EC=2.3.1.31 {ECO:0000313|EMBL:AWX45235.1};
GN Name=metX {ECO:0000313|EMBL:AWX45235.1};
GN ORFNames=HME9304_02247 {ECO:0000313|EMBL:AWX45235.1};
OS Allomuricauda aurantiaca.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=1383885 {ECO:0000313|EMBL:AWX45235.1, ECO:0000313|Proteomes:UP000248536};
RN [1] {ECO:0000313|EMBL:AWX45235.1, ECO:0000313|Proteomes:UP000248536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HME9304 {ECO:0000313|EMBL:AWX45235.1,
RC ECO:0000313|Proteomes:UP000248536};
RA Kang H., Kim H., Joh K.;
RT "Spongiibacterium sp. HME9304 Genome sequencing and assembly.";
RL Submitted (JUN-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-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005062}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056}.
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}.
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DR EMBL; CP030104; AWX45235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4LTH6; -.
DR KEGG; spon:HME9304_02247; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000248536; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04921; ACT_AKi-HSDH-ThrA-like_1; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR011147; Bifunc_aspartokin/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:SF3; HOMOSERINE DEHYDROGENASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AWX45235.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000248536};
KW Transferase {ECO:0000313|EMBL:AWX45235.1}.
FT DOMAIN 35..147
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 325..597
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 779..913
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 921..1122
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
SQ SEQUENCE 1128 AA; 124218 MW; AF4847930D0EAAAD CRC64;
MLQHINIPNF TTLSGNTQDL QLSYQLFGQE LHIAPIVLVN HALTGNSNVT GDGGWWTDIV
GDNKCIDTKK YTILAFNVPG NGYDGFVIDN YKDFVAGDIA NIFLDGLEEL KVEKLFAIIG
GSLGGGIAWE MVAFNPKITQ HLIPVASDWK STDWLIANCQ IQEQFLVNSK QPVHDARMHA
MLCYRTPESF KARFKRSTNE ELQVFNVESW LMHHGEKLQE RFQLSAYKLM NQLLKTIDIT
RNGGDAFDLI QKSDTKIHII GVNSDLFFTA EENKETFRNL AQANANVTYG EVQSLHGHDA
FLIEFQQLEN LLTPIFQKNG KKERIKILKF GGKSLANGEG LQNVLEIIAT RAKAGENFGV
VLSARGKATD QLEAMLDLAA KGKDFSEELQ TFSDYQSGAL SKIELKEELN HIAKLLKGVS
LTGDYSLKTK DELLSFGELI SGKVITSILS ESGVKAQLVD SRKLIKTDDT FNDAEVDEPI
SKENVIRYFQ ALDADIIPII TGFIASNKEG ETTTLGRNGS NYSAALLANF LDAQELVNYT
HVDGIFTANP DLVPEARLIR SISYAEANEL ANFGATILHA KTIIPLLEKN IPLRILNTFN
KNNKGTLIGA ETENGGIKSL SVLEHVALIN LEGRGLLGKV GVDARIFTVL GLNNINVGII
SQGSSERGIG LVVDSKQAQK AKRVLDIEFK TDYSNKDVNQ ITVLDDVAVI SIVGMDLSAF
HKPFNALAKN QVVPLLFNNT VSGKNVSLVV NSADLHKAVN VVHGQIFGIS KKVNLAIFGH
GNVGGTLIDQ ILSSQKSIEK RKGIDLRIFA VSNSRKTLLD VEGVNDTWRD DLENATGLHR
TKSIIEFAKK HHLENLIAID NTASESFVSN YEDLIANGFD LVSSNKIANT LGFDYYRTIR
GHLEKNQKQY LYETNVGAGL PLIDTIKLLH LSGENITRIK GVFSGSLSYI FNTFSENRIP
FSEIVKTAME KGYTEPDPRE DLSGNDVGRK LLILARELDL ENEFSDIQIE NLIPDTLQNV
GFENFMESIA SMDSGFSKIK NNQQQGHVLR YVGDLHGDLQ QEKGILDVKL ISVPKSSTLG
QVNGSDSIIE IYTESYGEHP LVIQGAGAGA AVTARGVFGD VLRIAEKM
//
