(data stored in SCRATCH zone)

SWISSPROT: A4ATL9_MARSH

ID   A4ATL9_MARSH            Unreviewed;       444 AA.
AC   A4ATL9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178103};
DE            EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS01178084};
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   OrderedLocusNames=FB2170_16931 {ECO:0000313|EMBL:EAR00789.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00789.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00789.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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|RuleBase:RU003664,
CC       ECO:0000256|SAAS:SAAS01178092}.
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:83898, ChEBI:CHEBI:83900,
CC         ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC         ECO:0000256|SAAS:SAAS01178088};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC       ECO:0000256|SAAS:SAAS00084431}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382026}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00639, ECO:0000256|SAAS:SAAS00569906}.
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DR   EMBL; CP002157; EAR00789.1; -; Genomic_DNA.
DR   RefSeq; WP_013304592.1; NC_014472.1.
DR   STRING; 313603.FB2170_16931; -.
DR   EnsemblBacteria; EAR00789; EAR00789; FB2170_16931.
DR   KEGG; fbc:FB2170_16931; -.
DR   eggNOG; ENOG4105DMZ; Bacteria.
DR   eggNOG; COG0771; LUCA.
DR   HOGENOM; HOG000049428; -.
DR   KO; K01925; -.
DR   OMA; VDKGNDY; -.
DR   OrthoDB; 1093223at2; -.
DR   BioCyc; MSP313603:G1GNS-164-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01087; murD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATL9.
DR   SWISS-2DPAGE; A4ATL9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459147};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084569};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459144};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459184};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084482};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459072};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459180, ECO:0000313|EMBL:EAR00789.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084387};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   DOMAIN      107    286       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      307    379       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     109    115       ATP. {ECO:0000256|HAMAP-Rule:MF_00639}.
SQ   SEQUENCE   444 AA;  49530 MW;  58F6C53037DB7E7B CRC64;
     MARLVILGGG ESGVGTAILG LKKGFEVFVS DKGKIKKKYK DVLEHIGINW EEEKHSKSVI
     LNADVVMKSP GIPDTVPLIK ELKEKLIPVI SEIEFAARYI DATIIGITGS NGKTTTTMLT
     NHIFKEEGLD VGMAGNIGDS FAKMVAENDH DNYVLEISSF QLDGINDFRP HIAIITNITP
     DHLDRYEYKF ENYVASKFRI AENQSKEDYL IYDADDEVIV EWLNKHPVKS ILMPFSIKNE
     LTQGAYLKND RIIIKTNNET LEMMTSTLAL EGKHNLKNTM AAATAAKLIG IRKETIRASI
     ANFQGAEHRL EKVLKIQHVQ YINDSKATNV NATYYALDSM SAPTVWIVGG VDKGNDYKEL
     MPLVREKVKA IICLGNDNSK IVDAFGNVVD LMVETYAMEE AVKVAYKIAE RGDTVLLSPA
     CASFDLFENY EDRGHQFKEA IKNL
//

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