DAPF2_NOSS1
ID DAPF2_NOSS1 Reviewed; 285 AA.
AC P54897;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Diaminopimelate epimerase 2 {ECO:0000255|HAMAP-Rule:MF_00197};
DE Short=DAP epimerase 2 {ECO:0000255|HAMAP-Rule:MF_00197};
DE EC=5.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00197};
DE AltName: Full=PLP-independent amino acid racemase 2 {ECO:0000255|HAMAP-Rule:MF_00197};
GN Name=dapF2 {ECO:0000255|HAMAP-Rule:MF_00197}; Synonyms=dapF;
GN OrderedLocusNames=alr4841;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9139910; DOI=10.1128/jb.179.9.2930-2937.1997;
RA Stricker O., Masepohl B., Klipp W., Boehme H.;
RT "Identification and characterization of the nifV-nifZ-nifT gene region from
RT the filamentous cyanobacterium Anabaena sp. strain PCC 7120.";
RL J. Bacteriol. 179:2930-2937(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00197}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00197}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00197}.
CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00197}.
CC -!- CAUTION: Could lack activity as the potential active site Cys residues
CC in positions 72 and 218 are both replaced by a Ser. {ECO:0000305}.
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DR EMBL; Z46907; CAA87006.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB76540.1; -; Genomic_DNA.
DR PIR; AI2410; AI2410.
DR PIR; S52295; S52295.
DR RefSeq; WP_010998969.1; NZ_RSCN01000037.1.
DR AlphaFoldDB; P54897; -.
DR SMR; P54897; -.
DR STRING; 103690.17133978; -.
DR EnsemblBacteria; BAB76540; BAB76540; BAB76540.
DR KEGG; ana:alr4841; -.
DR eggNOG; COG0253; Bacteria.
DR OMA; TIQIEIW; -.
DR OrthoDB; 1921631at2; -.
DR UniPathway; UPA00034; UER00025.
DR Proteomes; UP000002483; 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; IPR001653; DAP_epimerase_DapF.
DR PANTHER; PTHR31689; PTHR31689; 1.
DR Pfam; PF01678; DAP_epimerase; 2.
DR TIGRFAMs; TIGR00652; DapF; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Isomerase; Lysine biosynthesis;
KW Reference proteome.
FT CHAIN 1..285
FT /note="Diaminopimelate epimerase 2"
FT /id="PRO_0000149816"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT BINDING 209..210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT BINDING 219..220
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT SITE 160
FT /note="Could be important to modulate the pK values of the
FT two catalytic cysteine residues"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT SITE 209
FT /note="Could be important to modulate the pK values of the
FT two catalytic cysteine residues"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00197"
FT CONFLICT 223
FT /note="Missing (in Ref. 1; CAA87006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 31355 MW; AE1613FFEAD75063 CRC64;
MKFYKYHALG NDYLVINPQD LKFPLTPEKI KIICHRNFGI GSDGILLGPL ASTKAQFALR
IFNPDGSEAE KSGNGLRIFS RYLWDMGLVD EKPFSIETAG GIVESAIKDA GKTVQVEMGK
VSFWSRDIPV IGDDREVIQE KIFLDEGIFT FCAATIGNPH CVILLDDINS EVARNFGPIF
EGYPLFPNRT NVQFMKVLDR STIQIEIWER GAGYTLASGS SSSAAAATAH KLGLCDSKII
VKMPGGDILI QIKDDFHISM TDSVTKLAQG ELSTEIFAIE TVINI
