ID AK_MYCTU Reviewed; 421 AA. AC P0A4Z8; O69676; P47731; P97048; P97181; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-JUN-2009, entry version 29. DE RecName: Full=Aspartokinase; DE EC=2.7.2.4; DE AltName: Full=Aspartate kinase; DE Short=ASK; GN Name=ask; OrderedLocusNames=Rv3709c, MT3812; ORFNames=MTV025.057c; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RA Gilker J.M., Jucker M.T.; RT "Mycobacterium tuberculosis ask-alpha, ask-beta and asd genes."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. CC -!- ENZYME REGULATION: Feedback inhibition by lysine and threonine (By CC similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; tetrahydrodipicolinate from L-aspartate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 1/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 1/5. CC -!- SUBUNIT: Tetramer consisting of 2 isoforms Alpha (catalytic) and 2 CC isoforms Beta (function not known) (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Alpha; Synonyms=Aspartokinase subunit alpha; CC IsoId=P0A4Z8-1; Sequence=Displayed; CC Name=Beta; Synonyms=Aspartokinase subunit beta; CC IsoId=P0A4Z8-2; Sequence=VSP_018663; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the aspartokinase family. CC -!- SIMILARITY: Contains 2 ACT domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U90239; AAB49995.1; -; Genomic_DNA. DR EMBL; U90239; AAB49994.1; -; Genomic_DNA. DR EMBL; BX842583; CAA18031.1; -; Genomic_DNA. DR EMBL; AE000516; AAK48180.1; -; Genomic_DNA. DR PIR; F70794; F70794. DR RefSeq; NP_218226.1; -. DR RefSeq; NP_338366.1; -. DR GeneID; 885223; -. DR GeneID; 926450; -. DR GenomeReviews; AE000516_GR; MT3812. DR GenomeReviews; AL123456_GR; Rv3709c. DR KEGG; mtc:MT3812; -. DR KEGG; mtu:Rv3709c; -. DR TIGR; MT3812; -. DR TubercuList; Rv3709c; -. DR HOGENOM; P0A4Z8; -. DR OMA; P0A4Z8; MGKTTDN. DR BRENDA; 2.7.2.4; 809. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004072; F:aspartate kinase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR002912; ACT_bd. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kin_reg. DR InterPro; IPR018042; Aspartate_kinase_CS. DR Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 2. DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 3: Inferred from homology; KW Alternative initiation; Amino-acid biosynthesis; ATP-binding; KW Complete proteome; Diaminopimelate biosynthesis; Kinase; KW Lysine biosynthesis; Nucleotide-binding; Repeat; Transferase. FT CHAIN 1 421 Aspartokinase. FT /FTId=PRO_0000002385. FT DOMAIN 266 338 ACT 1. FT DOMAIN 348 413 ACT 2. FT VAR_SEQ 1 249 Missing (in isoform Beta). FT /FTId=VSP_018663. FT CONFLICT 288 336 DADVNIDMVLQNVSKVEDGKTDITFTCSRDVGPAAVEKLDS FT LRNEIGFS -> RRRRQHRHGAAERLQGRGRQDRHHLHLLP FT QTSGPPPWKNWTRSETRSAST (in Ref. 1; FT AAB49995). FT CONFLICT 383 421 IRISVLCRDTELDKAVVALHEAFGLGGDEEATVYAGTGR FT -> DQRSRCCAATPNWTRPWSRCMKRSGSAATRRPRCTRGR FT DGRWACQ (in Ref. 1; AAB49995/AAB49994). SQ SEQUENCE 421 AA; 44462 MW; 0567323B0D2085A7 CRC64; MALVVQKYGG SSVADAERIR RVAERIVATK KQGNDVVVVV SAMGDTTDDL LDLAQQVCPA PPPRELDMLL TAGERISNAL VAMAIESLGA HARSFTGSQA GVITTGTHGN AKIIDVTPGR LQTALEEGRV VLVAGFQGVS QDTKDVTTLG RGGSDTTAVA MAAALGADVC EIYTDVDGIF SADPRIVRNA RKLDTVTFEE MLEMAACGAK VLMLRCVEYA RRHNIPVHVR SSYSDRPGTV VVGSIKDVPM EDPILTGVAH DRSEAKVTIV GLPDIPGYAA KVFRAVADAD VNIDMVLQNV SKVEDGKTDI TFTCSRDVGP AAVEKLDSLR NEIGFSQLLY DDHIGKVSLI GAGMRSHPGV TATFCEALAA VGVNIELIST SEIRISVLCR DTELDKAVVA LHEAFGLGGD EEATVYAGTG R //