ID E6X5C1_CELAD Unreviewed; 1128 AA.
AC E6X5C1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Aspartate kinase {ECO:0000313|EMBL:ADV49457.1};
DE EC=1.1.1.3 {ECO:0000313|EMBL:ADV49457.1};
DE EC=2.7.2.4 {ECO:0000313|EMBL:ADV49457.1};
GN OrderedLocusNames=Celal_2162 {ECO:0000313|EMBL:ADV49457.1};
OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV49457.1, ECO:0000313|Proteomes:UP000008634};
RN [1] {ECO:0000313|EMBL:ADV49457.1, ECO:0000313|Proteomes:UP000008634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14237 / IC166 / ACAM 630
RC {ECO:0000313|Proteomes:UP000008634};
RX PubMed=21475589; DOI=10.4056/sigs.1543845;
RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL Stand. Genomic Sci. 4:72-80(2010).
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 3/3.
CC {ECO:0000256|ARBA:ARBA00005062}.
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; CP002453; ADV49457.1; -; Genomic_DNA.
DR RefSeq; WP_013550933.1; NC_014934.1.
DR AlphaFoldDB; E6X5C1; -.
DR STRING; 688270.Celal_2162; -.
DR KEGG; cao:Celal_2162; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_009116_7_1_10; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000008634; Chromosome.
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 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; 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; 1.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Kinase {ECO:0000313|EMBL:ADV49457.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADV49457.1}; Transferase {ECO:0000313|EMBL:ADV49457.1}.
FT DOMAIN 35..147
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 325..596
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 778..912
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 920..1121
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
SQ SEQUENCE 1128 AA; 124363 MW; EF213D16C2E485D0 CRC64;
MLQHLTIPNY TNHGGTTQDI NLSYQLFGPE LHTAPIVLVN HALTGSSEVA GENGWWSALI
GDGKCIDTQK YTILVFNVPG NGHDGFVVEN YKDFVAQDIA KLFLIGLKQL EVKRLFALIG
GSMGGGIAWE MIALEPNLTE NLIPVASDWK STDWLIANCQ IQEQFLLNSS QPVHDARMHA
MLCYRTPESF KERFKRSTNE ELHVFNVESW LTHHGAKLQE RFQLSAYKLM NQLLKSIDIT
RDNKDAFSTI EKSATNIHII GVDSDLFFTA QENKDTFKQL AQVNSNVTYG EIRSLHGHDA
FLIEFQQMEQ LLKGIFDQNG KNKRIKILKF GGRSLANGDG LNRVLEIVAT KVNKGENIGV
VLSARGKATD HLESILKRAA KGKEYSKDFE AFKVYQQSDF NVALSKEFSD LEKLFEGVSL
LGDYSAKIKD QVLSFGELIS GKVITQLLKA NGVKAKFIDS RELIKTDSNF GDAQVYEALS
KENVLEVISK LDANVVPVIT GFIASNKGGE TTTLGRNGSN YSAALIANFL DAAELQNYTH
VDGIYTANPD YVADAKRIAE LSYGEANELA NFGATILHAK TIIPLIEKNI PLRILNTFNG
DNEGTLISAK TSKEGIKSLS VIENVALVNF EGRGLLGKVG VDARVFKTLG ANNISVNIIS
QGSSERGLGF VVDADKAEKA KEVLIDEFSS DFQTKDVNMI TVTKDVSVIS IVGQDLSSFH
KPFNELIKNQ IVPLLFNNTV TGKNVSLVVR RKDLYKALNV MHGQVFGISK KVNLAIFGHG
NVGGTLIDQI LKSAQNIEER KGIQLKVFAV ANSKKVLLNK NGISENWKTD LDDQGVAFDL
NSIFDFAKSH HLENLIAVDN TASKTFVASY LNMIENGFDL VSSNKIANTL SFDFYQNLRT
ELEKSQKQYL YETNVGAGLP LIDTIKLLHL SGENITRIKG VFSGSLSYIF NTFSEVDRPF
SSILKEAMEK GFTEPDARED LSGNDVGRKL LILARELDLS NEFADISIQN LIPESLHNVT
VDEFKSKLSS LDAIFEKIKK EQKPNHVLRY VGDLSGDLQK EKGNLEVKLV SVPKESALGQ
VKGSDSIIEI YTESYGENPL VIQGAGAGAA VTARGVFGDI LRIIEKGK
//
