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Database: UniProt
Entry: A0A076MYF1_AMYME
LinkDB: A0A076MYF1_AMYME
Original site: A0A076MYF1_AMYME 
ID   A0A076MYF1_AMYME        Unreviewed;       464 AA.
AC   A0A076MYF1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   05-DEC-2018, entry version 21.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|SAAS:SAAS00382177};
DE            EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|SAAS:SAAS00382044};
DE   AltName: Full=D-glutamic acid-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00639};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_00639};
GN   Name=murD {ECO:0000256|HAMAP-Rule:MF_00639,
GN   ECO:0000313|EMBL:AIJ22617.1};
GN   ORFNames=AMETH_2525 {ECO:0000313|EMBL:AIJ22617.1};
OS   Amycolatopsis methanolica 239.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ22617.1, ECO:0000313|Proteomes:UP000062973};
RN   [1] {ECO:0000313|EMBL:AIJ22617.1, ECO:0000313|Proteomes:UP000062973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=239 {ECO:0000313|EMBL:AIJ22617.1,
RC   ECO:0000313|Proteomes:UP000062973};
RA   Tang B.;
RT   "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|SAAS:SAAS00382010}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-
CC         alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-
CC         muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216, ChEBI:CHEBI:83898,
CC         ChEBI:CHEBI:83900; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00639, ECO:0000256|SAAS:SAAS00382107};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|SAAS:SAAS00382165}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|SAAS:SAAS00084461}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00639, ECO:0000256|SAAS:SAAS00569906}.
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DR   EMBL; CP009110; AIJ22617.1; -; Genomic_DNA.
DR   RefSeq; WP_017981837.1; NZ_CP009110.1.
DR   EnsemblBacteria; AIJ22617; AIJ22617; AMETH_2525.
DR   KEGG; amq:AMETH_2525; -.
DR   PATRIC; fig|1068978.7.peg.2698; -.
DR   KO; K01925; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000062973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00639; MurD; 1.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01087; murD; 1.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084371};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459080};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084380};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084500};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459111};
KW   Complete proteome {ECO:0000313|Proteomes:UP000062973};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084399};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084447, ECO:0000313|EMBL:AIJ22617.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459201};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062973}.
FT   DOMAIN        6     49       AlaDh_PNT_C. {ECO:0000259|Pfam:PF01262}.
FT   DOMAIN      110    291       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   NP_BIND     112    118       ATP. {ECO:0000256|HAMAP-Rule:MF_00639}.
SQ   SEQUENCE   464 AA;  47616 MW;  E00197FAACBFFB02 CRC64;
     MFAGRNVLVA GAGVTGRSAV RALTERGARV TVTDGNAERL AELDGLGAEL APGLTEPPAG
     TDLVVTSPGW RPTAPLLVAS AAAGIEVIGD VELAWRASRD LPNPATWLAV TGTNGKTTTV
     GMLESMLRAG GVHALACGNI GLPVLDAVFE GYEALAVELS SFQLHWSSTL APHASVVLNL
     AEDHLDWHGT MESYAAAKGT IHAHSNVVVH NSDDPWSVRL AGEYAPAGAK RVGFRLDTPR
     PGELGLVEDL LIDRAYGPDP QHSADELISV SEVRPAGPHN LANALAAAAL ARAYGIDPAG
     VAKGLREFQP GAHRAVEVGE FGGVRYVNDS KATNPHAAAG SLLAHSSVVW IAGGQLKGAA
     VDELVEVVAG RLRGVVLMGA DAPVIAAALA RHAPDVPVHR VASGDDGAMN EAVSVASDLA
     RPGDVVLLAP AGASLDMFRN YAHRGDAFAD AVLARASGSA DDGR
//
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