ID A0A162MV45_9FIRM Unreviewed; 452 AA.
AC A0A162MV45;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:KYO67791.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KYO67791.1};
GN Name=algC {ECO:0000313|EMBL:KYO67791.1};
GN ORFNames=ATZ99_04310 {ECO:0000313|EMBL:KYO67791.1};
OS Thermovenabulum gondwanense.
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermovenabulum.
OX NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO67791.1, ECO:0000313|Proteomes:UP000075737};
RN [1] {ECO:0000313|EMBL:KYO67791.1, ECO:0000313|Proteomes:UP000075737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R270 {ECO:0000313|EMBL:KYO67791.1,
RC ECO:0000313|Proteomes:UP000075737};
RA Patel B.K.;
RT "Draft genome of Thermovenabulum gondwanense isolated from a red
RT thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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:KYO67791.1}.
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DR EMBL; LOHZ01000020; KYO67791.1; -; Genomic_DNA.
DR RefSeq; WP_068747608.1; NZ_LOHZ01000020.1.
DR AlphaFoldDB; A0A162MV45; -.
DR STRING; 520767.ATZ99_04310; -.
DR PATRIC; fig|520767.4.peg.441; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000075737; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KYO67791.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000075737}.
FT DOMAIN 7..138
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 153..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 255..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 370..446
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 452 AA; 50424 MW; 0C07CFDCB0F88405 CRC64;
MHRFNPNIFR QYDIRGIVGE ELNEDVAQTL GKAFGSFSIK NGEKLVVVGS DNRLSSPSLK
KAVINGLLST GCDVVDLGTV VTPIFYFARI HYKINPGIMV TASHNPPQFN GFKVAFGHAT
LYGEDIQYIR KLMEEGNFEK GNGTLSFIDP TEDYISDITS RIKLSRPLKV AIDCGNGTAS
HIAERLFTRL GAQVYPLYCD SDPNFPNHFP DPVKPENMED LKNLVLKGNL DLGIGFDGDG
DRIGVVDDKG QIIWGDMLMI LFWREILPKH PGATAIVEVK CSQALVEEIL KMGGNPIFYK
TGHSLIKAKM KEIGAIFTGE MSGHMFFADE YYGFDDALYA AARLLRILSN TEKKLSELLS
DVPKYYSTPE IRVHCSDEEK FDKVQEVKKY FSGRYEIIDI DGARVIFPDG WGLVRASNTG
PELIVRCESK TPEGLEKIKE EIKSALSPLK VF
//
