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Database: UniProt
Entry: K9TLD6_9CYAN
LinkDB: K9TLD6_9CYAN
Original site: K9TLD6_9CYAN 
ID   K9TLD6_9CYAN            Unreviewed;       367 AA.
AC   K9TLD6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=Oscil6304_3396 {ECO:0000313|EMBL:AFY82966.1};
OS   Oscillatoria acuminata PCC 6304.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY82966.1, ECO:0000313|Proteomes:UP000010367};
RN   [1] {ECO:0000313|EMBL:AFY82966.1, ECO:0000313|Proteomes:UP000010367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY82966.1,
RC   ECO:0000313|Proteomes:UP000010367};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Oscillatoria acuminata PCC 6304.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634603-3,
CC         ECO:0000256|RuleBase:RU366006};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR634603-3,
CC       ECO:0000256|RuleBase:RU366006};
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. {ECO:0000256|ARBA:ARBA00008031,
CC       ECO:0000256|RuleBase:RU366006}.
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DR   EMBL; CP003607; AFY82966.1; -; Genomic_DNA.
DR   RefSeq; WP_015149596.1; NC_019693.1.
DR   AlphaFoldDB; K9TLD6; -.
DR   STRING; 56110.Oscil6304_3396; -.
DR   KEGG; oac:Oscil6304_3396; -.
DR   PATRIC; fig|56110.3.peg.4068; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_3_3; -.
DR   InParanoid; K9TLD6; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000010367; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:UniProtKB-UniRule.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   CDD; cd03319; L-Ala-DL-Glu_epimerase; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR034593; DgoD-like.
DR   InterPro; IPR034603; Dipeptide_epimerase.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF3; ENOLASE SUPERFAMILY MEMBER DDB_G0284701; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDG00180; muconate_cycloisomerase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU366006};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR634603-3, ECO:0000256|RuleBase:RU366006};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634603-3,
KW   ECO:0000256|RuleBase:RU366006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010367}.
FT   DOMAIN          160..252
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        175
FT                   /note="Proton acceptor; specific for (R)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   ACT_SITE        278
FT                   /note="Proton acceptor; specific for (S)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ   SEQUENCE   367 AA;  39591 MW;  8E56BCF57CC21260 CRC64;
     MKIQIETFTV HKRFALTISR GTTAQSTNVL VKVEAEGITG WGEASPFSAG GTPQTTSEIV
     AALQEVAPKL AGFSPFDRQE IEAFLMRLTT EGKFPSAAQA GLDTALQDWL GKKVGLPLWQ
     LWGLDCNRIV PTSLTIGISS PEAARTRVRH WFNLDSDSPE TEAVPSTQGC AIKVKLGSPA
     GIAADRAMFL AVQEEAPPGS GFSIDANGGW TLEDAIAMSH WLSTRGVKYL EQPLPVAAQE
     ELRHLYRESP LPIFVDESCF TRADIIPLAD RVHGINIKLM KCGGLTEAMG MIHTAHACGL
     QVMFGCYSDT VVANTALSHL SPLADYLDLD SHLNLIDDPF TGAIVQDGRL LPNDLPGLGV
     QHRAYNS
//
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