GenomeNet

Database: UniProt
Entry: I1XGH6_METNJ
LinkDB: I1XGH6_METNJ
Original site: I1XGH6_METNJ 
ID   I1XGH6_METNJ            Unreviewed;       282 AA.
AC   I1XGH6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Diaminopimelate epimerase {ECO:0000256|ARBA:ARBA00013080, ECO:0000256|HAMAP-Rule:MF_00197};
DE            Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE            EC=5.1.1.7 {ECO:0000256|ARBA:ARBA00013080, ECO:0000256|HAMAP-Rule:MF_00197};
DE   AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197};
GN   Name=dapF {ECO:0000256|HAMAP-Rule:MF_00197};
GN   OrderedLocusNames=Q7A_649 {ECO:0000313|EMBL:AFI83495.1};
GN   ORFNames=CDW43_02980 {ECO:0000313|EMBL:AUZ83593.1};
OS   Methylophaga nitratireducenticrescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI83495.1, ECO:0000313|Proteomes:UP000009144};
RN   [1] {ECO:0000313|EMBL:AFI83495.1, ECO:0000313|Proteomes:UP000009144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI83495.1,
RC   ECO:0000313|Proteomes:UP000009144};
RX   PubMed=22815445; DOI=10.1128/JB.00726-12;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT   sp. strain JAM7.";
RL   J. Bacteriol. 194:4126-4127(2012).
RN   [2] {ECO:0000313|EMBL:AFI83495.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI83495.1};
RX   PubMed=23148104; DOI=10.1099/ijs.0.044545-0;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Methylophaga nitratireducenticrescens sp. nov. and Methylophaga frappieri
RT   sp. nov., isolated from the biofilm of the methanol-fed denitrification
RT   system treating the seawater at the Montreal Biodome.";
RL   Int. J. Syst. Evol. Microbiol. 63:2216-2222(2013).
RN   [3] {ECO:0000313|EMBL:AFI83495.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI83495.1};
RA   Villeneuve C., Villemur R.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AUZ83593.1, ECO:0000313|Proteomes:UP000238402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP59 {ECO:0000313|EMBL:AUZ83593.1,
RC   ECO:0000313|Proteomes:UP000238402};
RA   Villemur R.;
RT   "The sequence of the genome of Methylophaga nitratireducenticrescens GP59
RT   and its two plasmids.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate
CC       (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-
CC       lysine and an essential component of the bacterial peptidoglycan.
CC       {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-
CC         diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:57791; EC=5.1.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000599, ECO:0000256|HAMAP-
CC         Rule:MF_00197};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005196, ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC       {ECO:0000256|ARBA:ARBA00010219, ECO:0000256|HAMAP-Rule:MF_00197}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003390; AFI83495.1; -; Genomic_DNA.
DR   EMBL; CP021973; AUZ83593.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1XGH6; -.
DR   STRING; 754476.Q7A_649; -.
DR   KEGG; mej:Q7A_649; -.
DR   PATRIC; fig|754476.3.peg.639; -.
DR   eggNOG; COG0253; Bacteria.
DR   HOGENOM; CLU_053306_1_1_6; -.
DR   OrthoDB; 9805408at2; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000009144; Chromosome.
DR   Proteomes; UP000238402; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00197; DAP_epimerase; 1.
DR   InterPro; IPR018510; DAP_epimerase_AS.
DR   InterPro; IPR001653; DAP_epimerase_DapF.
DR   NCBIfam; TIGR00652; DapF; 1.
DR   PANTHER; PTHR31689:SF0; DIAMINOPIMELATE EPIMERASE; 1.
DR   PANTHER; PTHR31689; DIAMINOPIMELATE EPIMERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01678; DAP_epimerase; 2.
DR   SUPFAM; SSF54506; Diaminopimelate epimerase-like; 1.
DR   PROSITE; PS01326; DAP_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00197}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00197};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW   Rule:MF_00197}.
FT   ACT_SITE        74
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10125"
FT   ACT_SITE        74
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   ACT_SITE        219
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         75..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         210..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         220..221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            161
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            210
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            270
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
SQ   SEQUENCE   282 AA;  30717 MW;  4F2DD1B44E28B5A4 CRC64;
     MLKFSKMHGL GNDFVVIDAI NQSVQLTTEQ IRFMADRHIG IGCDQLLLVE NSDLKDVDFR
     YRIFNADGGE VSQCGNGARC FARYVRDNGL TTKDSIAVET ASGVIYPILQ ADGQVCVDMG
     KPRFSPEQVP FNVAEQSNTY MLAVEPGRQV EIAALSMGNP HAVLLVDDVT TAPVGELGPK
     IENHQQFPER VNVGFMQLVD HEHIKLRVYE RGSAETTACG TGACAAVVSG IRRGILGRQV
     SVLLPGGTLE ISWPDENSSV WMTGPAQHVF DGEIAWATLN NL
//
DBGET integrated database retrieval system