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Database: UniProt
Entry: K9VD58_9CYAN
LinkDB: K9VD58_9CYAN
Original site: K9VD58_9CYAN 
ID   K9VD58_9CYAN            Unreviewed;       355 AA.
AC   K9VD58;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=Osc7112_0826 {ECO:0000313|EMBL:AFZ05407.1};
OS   Oscillatoria nigro-viridis PCC 7112.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ05407.1, ECO:0000313|Proteomes:UP000010478};
RN   [1] {ECO:0000313|EMBL:AFZ05407.1, ECO:0000313|Proteomes:UP000010478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ05407.1,
RC   ECO:0000313|Proteomes:UP000010478};
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 sp. PCC 7112.";
RL   Submitted (MAY-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; CP003614; AFZ05407.1; -; Genomic_DNA.
DR   RefSeq; WP_015174736.1; NC_019729.1.
DR   AlphaFoldDB; K9VD58; -.
DR   STRING; 179408.Osc7112_0826; -.
DR   KEGG; oni:Osc7112_0826; -.
DR   PATRIC; fig|179408.3.peg.1030; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_3_3; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000010478; 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; SFLDF00010; dipeptide_epimerase; 1.
DR   SFLD; SFLDS00001; Enolase; 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:UP000010478}.
FT   DOMAIN          150..244
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        166
FT                   /note="Proton acceptor; specific for (R)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   ACT_SITE        270
FT                   /note="Proton acceptor; specific for (S)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   BINDING         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ   SEQUENCE   355 AA;  39153 MW;  56B8DC7DAB491591 CRC64;
     MHVQIETFTV RKRFALTISR GTTAQSTNLW VKLAHEGIEG WGEASPFSTG SRPQTTEILL
     AALQEVAPLL EKLTPFDRQK VEQVLTEVNL PSAARAGIDM AMHDWLGKKA GLPLWKMWGL
     DRSRIVPTSV TIGINSPRSA RERVRDWFGK DATVPGSLKY RAVKVKLGNP EGIEADKAML
     IAVRDEAPTN IQISVDANGG WSLTSAIEMC RWLEKYRINY VEQPLSPVAD MDEFSELYRK
     SPLPIFADES CFNSSDIPKL AHCVHGINIK MMKSGGLTEA MRMIHTAKAC NLQVMFGCYS
     DSAIANTAAA QLSPLADYLD LDSHLNLLDD PFSGAIVENG CLLPNERSGL GVRRI
//
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