ID A0A0C1L882_9BACT Unreviewed; 185 AA.
AC A0A0C1L882;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|ARBA:ARBA00031828, ECO:0000256|PIRNR:PIRNR004682};
DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR004682};
GN ORFNames=HY58_06230 {ECO:0000313|EMBL:KIC91808.1};
OS Flavihumibacter sp. ZG627.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1463156 {ECO:0000313|EMBL:KIC91808.1, ECO:0000313|Proteomes:UP000031400};
RN [1] {ECO:0000313|EMBL:KIC91808.1, ECO:0000313|Proteomes:UP000031400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZG627 {ECO:0000313|EMBL:KIC91808.1,
RC ECO:0000313|Proteomes:UP000031400};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter carbonis ZG627.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR004682-4};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR004682-4};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR004682}.
CC -!- SIMILARITY: Belongs to the gmhB family.
CC {ECO:0000256|PIRNR:PIRNR004682}.
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:KIC91808.1}.
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DR EMBL; JPHF01000002; KIC91808.1; -; Genomic_DNA.
DR RefSeq; WP_039129257.1; NZ_JPHF01000002.1.
DR AlphaFoldDB; A0A0C1L882; -.
DR STRING; 1463156.HY58_06230; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000031400; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004446; Heptose_bisP_phosphatase.
DR InterPro; IPR006543; Histidinol-phos.
DR InterPro; IPR013954; PNK3P.
DR NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR NCBIfam; TIGR01656; Histidinol-ppas; 1.
DR PANTHER; PTHR42891; D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE; 1.
DR PANTHER; PTHR42891:SF1; D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE; 1.
DR Pfam; PF08645; PNK3P; 1.
DR PIRSF; PIRSF004682; GmhB; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR004682};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR004682};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR004682};
KW Magnesium {ECO:0000256|PIRSR:PIRSR004682-4};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004682-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000031400};
KW Zinc {ECO:0000256|PIRSR:PIRSR004682-4}.
FT ACT_SITE 16
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT ACT_SITE 18
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT SITE 60
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT SITE 109
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT SITE 110
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
SQ SEQUENCE 185 AA; 21335 MW; 3B29BE941016266C CRC64;
MIKLHEIDKS WSLFLDRDGV INHEKHLDYI YNYAEFVYYE GVEEAMTTFA RNFGKIFIVT
NQRGVGKGLM TESDLNDIHR KMVERFQELH CNIDAIYYCT SLDNSHPDRK PNPGMAFRAK
EDYPEIDLSK SIVVGNNLSD MEFGRNAGML TVFVQTTHPH QPLPHPLIDL AFKDLLNFSR
ALPPA
//
