ID Q0YQU6_9CHLB Unreviewed; 1053 AA.
AC Q0YQU6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=HAD-superfamily hydrolase subfamily IA, variant 3:Beta-phosphoglucomutase hydrolase {ECO:0000313|EMBL:EAT58631.1};
GN ORFNames=CferDRAFT_0605 {ECO:0000313|EMBL:EAT58631.1};
OS Chlorobium ferrooxidans DSM 13031.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=377431 {ECO:0000313|EMBL:EAT58631.1, ECO:0000313|Proteomes:UP000004162};
RN [1] {ECO:0000313|EMBL:EAT58631.1, ECO:0000313|Proteomes:UP000004162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58631.1,
RC ECO:0000313|Proteomes:UP000004162};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Chlorobium ferroxidans DSM
RT 13031.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT58631.1, ECO:0000313|Proteomes:UP000004162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58631.1,
RC ECO:0000313|Proteomes:UP000004162};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Chlorobium ferroxidans DSM
RT 13031.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR610972-3};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR610972-3};
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:EAT58631.1}.
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DR EMBL; AASE01000015; EAT58631.1; -; Genomic_DNA.
DR RefSeq; WP_006366689.1; NZ_AASE01000015.1.
DR AlphaFoldDB; Q0YQU6; -.
DR OrthoDB; 9758855at2; -.
DR Proteomes; UP000004162; Unassembled WGS sequence.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02598; HAD_BPGM; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR010972; Beta-phosphoglucomutase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EAT58631.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000004162}.
FT DOMAIN 261..515
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 570..970
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 982..1043
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 11..13
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 59..64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 137..141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 137
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-4"
FT SITE 172
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-4"
SQ SEQUENCE 1053 AA; 118556 MW; 13D72CD51B6428EF CRC64;
MSNLFKGAIF DLDGVITGTA KVHSLAWESM FNFFLKNHAE INNEPYVPFD PAHDYHKYVD
GKPRMEGVKS FLASRDIELP FGELDDNPEK ETVCGLGNRK NSLFTEILIK EGPEVYTSSV
ELINNLIAKG VRIGIASSSR NCQLILKLSK LEHLFETRVD GEVSIVMGLK GKPNPDIFVT
AARNLGLEPH ECVVVEDAIS GVQAGSRGNF GMVLGIARDI EGGKLKENGA DIVVRDLAEI
TIEEIEQWFT DGLEHEGWNL TYTEFSPKDE KLRETLTSTG NGYLGVRGTY EGSSISHHHY
PGTYIAGIFN KLPSDVHGQT IFNNDFVNTP NWLPIEFRIG GGEFIDPFEQ KILSYHQNLS
LSDGSMERTL VIQDNLGRLT KITSRRFASM DDPHRCALKF TLKPVNYSAT VEFRSSIDGR
IQNKGVARYS ELSCDHLDHV GSAADQKSML LHVRTNVSHY EIVTAARTRV LSHGKQIEPK
RTVISESRYI GELFQLHLTP EKSCTIEKLV TIHTSLDHNS TDALKAARAA VEKEVSFDAL
LEASTAAWKK IWAKADIQIE GDRYSQKLLR LHTYHMLCTA SPHNPSIDAG MPARGLNGEA
YRGHIFWDEI FILPFFNRHF PEISKALLMY RFNRLDAARE YARENGYKGA MFPWQTADDG
HEDTQIIHFN PKSGHWGPDL SRMQRHVSIA VFYNVWRYIY DTGDTDFLNA CGAELMFEIA
RFWASIAHHS AETGKYHIEG VMGPDEFHET LPGSGKEGLK DNAYTNIMTV WLLGKAVEIG
ETIDPAILRH LIEKIHLGFD ELQQWRDISN NLNILIDEAG VIEQFDGYMG LKELDWKHYR
TTYGNIHRMD RILKAEGDSP DLYKVAKQPD VLMTFYTLSP GEVAELLGKI GYRLPDSFTL
VRNNYAYYEP RTSHGSTLSK VVHSIISSYL EDGHEMAWKW FAEALKSDIE DTQGGTTQEG
IHCGVMAGTL DTVTRYFAGI SFYNEKLNVH PNLPDQWKKL TLNVCFRNNS YTIAISRNNV
EVTLIDAAES TIPACIVGEH ITLKKGVAYH SAK
//
