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Database: UniProt/TrEMBL
Entry: B4RR79_NEIG2
LinkDB: B4RR79_NEIG2
Original site: B4RR79_NEIG2 
ID   B4RR79_NEIG2            Unreviewed;       305 AA.
AC   B4RR79;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   26-NOV-2014, entry version 47.
DE   RecName: Full=Homoserine kinase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000256|SAAS:SAAS00085804};
DE            Short=HK {ECO:0000256|HAMAP-Rule:MF_00301};
DE            Short=HSK {ECO:0000256|HAMAP-Rule:MF_00301};
DE            EC=2.7.1.39 {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000256|SAAS:SAAS00085809};
GN   Name=thrB {ECO:0000256|HAMAP-Rule:MF_00301};
GN   OrderedLocusNames=NGK_2537 {ECO:0000313|EMBL:ACF31137.1};
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=521006 {ECO:0000313|EMBL:ACF31137.1, ECO:0000313|Proteomes:UP000002564};
RN   [1] {ECO:0000313|EMBL:ACF31137.1, ECO:0000313|Proteomes:UP000002564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945 {ECO:0000313|EMBL:ACF31137.1,
RC   ECO:0000313|Proteomes:UP000002564};
RX   PubMed=18586945; DOI=10.1128/JB.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L-
CC       homoserine. {ECO:0000256|HAMAP-Rule:MF_00301,
CC       ECO:0000256|SAAS:SAAS00085813}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 4/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00301, ECO:0000256|SAAS:SAAS00085805}.
CC   -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family.
CC       {ECO:0000256|HAMAP-Rule:MF_00301}.
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DR   EMBL; CP001050; ACF31137.1; -; Genomic_DNA.
DR   RefSeq; WP_003690378.1; NC_011035.1.
DR   RefSeq; YP_002003162.1; NC_011035.1.
DR   STRING; 521006.NGK_2537; -.
DR   EnsemblBacteria; ACF31137; ACF31137; NGK_2537.
DR   GeneID; 6449613; -.
DR   KEGG; ngk:NGK_2537; -.
DR   PATRIC; 20343854; VBINeiGon87511_2755.
DR   eggNOG; COG2334; -.
DR   HOGENOM; HOG000004810; -.
DR   KO; K02204; -.
DR   OMA; NAWCFEP; -.
DR   OrthoDB; EOG6BW4W1; -.
DR   BioCyc; NGON521006:GJ73-2610-MONOMER; -.
DR   UniPathway; UPA00050; UER00064.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00301; Homoser_kinase_2; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR005280; Homoserine_kinase_ThrB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR00938; thrB_alt; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00301,
KW   ECO:0000256|SAAS:SAAS00085810};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00301,
KW   ECO:0000256|SAAS:SAAS00085806};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002564};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00301,
KW   ECO:0000256|SAAS:SAAS00085814};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301,
KW   ECO:0000256|SAAS:SAAS00085815};
KW   Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00301,
KW   ECO:0000256|SAAS:SAAS00085807};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00301,
KW   ECO:0000256|SAAS:SAAS00085812}.
SQ   SEQUENCE   305 AA;  33596 MW;  C56B5FBF0DF4ECA3 CRC64;
     MSVYTSVSDD EMRGFLSGYD LGEFVSLQGI AQGITNSNYF LTTTSGRYVL TVFEVLKQEE
     LSFFLELNRH LSMKGVAVAA PVARKDGRLD SVLAGKPACL VACLKGSDTA LPTAEQCFHT
     GAMLAKMHLA AADFPLEMEN PRYDAWWTEA CARLLPVLSQ DDAALLCSEI DALKDNLGNH
     LPSGIIHADL FKDNVLLDGG QVSGFIDFYY ACRGNFMYDL AIAVNDWART ADNKLDEALK
     KAFIGGYEGV RPLSAGEKAY FPTAQRAGCI RFWVSRLLDF HFPQAGEMTF IKDPNAFRNL
     LLSLD
//
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