ID U5Q6T6_9BACT Unreviewed; 809 AA.
AC U5Q6T6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Bifunctional aspartokinase/homoserine dehydrogenase 1 {ECO:0000313|EMBL:AGY54236.1};
DE EC=1.1.1.3 {ECO:0000313|EMBL:AGY54236.1};
DE EC=2.7.2.4 {ECO:0000313|EMBL:AGY54236.1};
GN ORFNames=BRDCF_p1609 {ECO:0000313|EMBL:AGY54236.1};
OS Bacteroidales bacterium CF.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY54236.1, ECO:0000313|Proteomes:UP000017642};
RN [1] {ECO:0000313|EMBL:AGY54236.1, ECO:0000313|Proteomes:UP000017642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AGY54236.1};
RX PubMed=24356833;
RA Tang S., Edwards E.A.;
RT "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT Dechlorinating Enrichment Culture.";
RL Genome Announc. 1:e01066-13(2013).
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}.
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DR EMBL; CP006772; AGY54236.1; -; Genomic_DNA.
DR AlphaFoldDB; U5Q6T6; -.
DR STRING; 1400053.BRDCF_p1609; -.
DR KEGG; bacc:BRDCF_p1609; -.
DR HOGENOM; CLU_009116_7_1_10; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000017642; Chromosome.
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; 3.40.1160.10; 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; 2.
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:AGY54236.1};
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:AGY54236.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017642};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGY54236.1}.
FT DOMAIN 319..388
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 400..484
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 809 AA; 88825 MW; CA0D20662BCD8885 CRC64;
MQVLKFGGSS VADAANISNV VKIVRESVKK DRTILVASAI GGCTDKLIEI GKLAAMQDES
YNELIDKLEE RHQKIIWELL PIDYQHALSS KTKNTFNQLR EICKGVFYLK ELSNSSLDLI
MSFGEVLSTR IISERFSSMG INNFWADARE IIKTEPGSSG NVVIKQISYS NIKKTLSSNR
QRLIIVPGFI ASDILKRTTT LGRGGSDYTA ALLAEATDAR ELQIWSDVNG MMTADPRIVP
EAITIRHISY KEAQELSHFG AKVIYPPTIQ PAVSKGIPIV VKNTFDPEDP GTVIENNPPE
SRGKIRGISR SNKIALLSME GSGMVGVPGY SARLFSALAN AGVNIVLITQ ASSVHTMCVA
IEDSDAEKAK KAADGVFAYE ISLNRVNPLK VERGFSIISL VGDDLKNQSG TGGKMFNAIG
RSGINIRAIA QGSSEKNISV VVKEEDSDLS IKVIHEEFFG EEKKKLNLFI AGYGQVAKAL
LSIIDSRRDW LFSKKGLEIS IVAICNSKKM ISDKRGIQIK QIKSLLPLGE PSDINRFREI
CCDMSLPESL FVDCTADRSV TSLYQEFLQS GCKVVTCNKI GLSSSQESYD ALQEICINTG
IQLRYETTVG AALPVISTIR GRRECGDNIQ RVEAILSGTL NYLFSKYDGS VRFTDLVEQA
RRAGYTEPDP RIDLAGTDTM RKALILARES GFRLEPDEIE IRPFLNEALF SADIDIFYAK
LRDYEEKIAA RFRESEAKGE RLRFIAKIDK EGCSIGLESI GSSHPFYNIC GRDNSVMIYS
DEYTSPLIVT GAGAGASLTA SGIFSDLLA
//