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Database: UniProt
Entry: M3G5H2_9LEPT
LinkDB: M3G5H2_9LEPT
Original site: M3G5H2_9LEPT 
ID   M3G5H2_9LEPT            Unreviewed;       321 AA.
AC   M3G5H2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Metalloenzyme domain protein {ECO:0000313|EMBL:EMF81209.1};
GN   ORFNames=LEP1GSC188_2664 {ECO:0000313|EMBL:EMF81209.1};
OS   Leptospira weilii serovar Topaz str. LT2116.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1088540 {ECO:0000313|EMBL:EMF81209.1, ECO:0000313|Proteomes:UP000011770};
RN   [1] {ECO:0000313|EMBL:EMF81209.1, ECO:0000313|Proteomes:UP000011770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2116 {ECO:0000313|EMBL:EMF81209.1,
RC   ECO:0000313|Proteomes:UP000011770};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA   Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA   Nierman W.C., Fouts D.E.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC       {ECO:0000256|ARBA:ARBA00010373}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMF81209.1}.
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DR   EMBL; AHOR02000037; EMF81209.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3G5H2; -.
DR   Proteomes; UP000011770; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008973; F:phosphopentomutase activity; IEA:InterPro.
DR   GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR010045; DeoB.
DR   InterPro; IPR006124; Metalloenzyme.
DR   PANTHER; PTHR21110; PHOSPHOPENTOMUTASE; 1.
DR   PANTHER; PTHR21110:SF0; PHOSPHOPENTOMUTASE; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011770}.
FT   DOMAIN          195..308
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   321 AA;  36575 MW;  A2AC7E65EE8EE3DE CRC64;
     MIFYMFIDGV GFGPDDPETN PFSRYANSFF LPLAGKPIPE NAPESLKNTI FLKTDASMGI
     KGLPQSATGQ TSLWTGINAC KILQRHLSGF PTFTLKKIIS KYSIIRVLEE HGFKADLLNC
     YTPAFNEHVK KNPRHLSAST LIQMASDKPL KGMEDLRQGK GLYMDITHEY LKEFSKGYLD
     DSDELFQIRD PYKTGKSIIR NCKEDNYTLC IYEFFLTDKV GHKMHWEAAQ KYIGELEDFL
     TGVLEELNPE EDQLVVTSDH GNIEDLSVDV HTLNQVPTIL YGKYTSQMEK KIRSIVDIPS
     AIYDVLGIDI ELRDEEFMKT E
//
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