ID F4LW67_TEPAE Unreviewed; 451 AA.
AC F4LW67;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:CDI40460.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:CDI40460.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CDI40460.1};
GN Name=algC {ECO:0000313|EMBL:CDI40460.1};
GN OrderedLocusNames=TEPIRE1_0713 {ECO:0000313|EMBL:CDI40460.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CDI40460.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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}.
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DR EMBL; HF563609; CDI40460.1; -; Genomic_DNA.
DR RefSeq; WP_013777766.1; NC_019954.2.
DR AlphaFoldDB; F4LW67; -.
DR STRING; 1209989.TepRe1_0656; -.
DR KEGG; tae:TepiRe1_0713; -.
DR KEGG; tep:TepRe1_0656; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_9; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000010802; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase 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:CDI40460.1};
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:UP000010802}.
FT DOMAIN 7..126
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 151..249
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 254..364
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 369..445
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 451 AA; 50536 MW; FECC7CC9A7917388 CRC64;
MKINPYIFRQ YDIRGVVGED LDENFARRLG QAFGTYTLKN NETSVIVGCD NRISSPSLKK
AVTEGLLSTG CNVVDIGTVV TPIFYYARIH FNINPGIMVT ASHNPAQFNG FKVAFGPGTI
YGDEIQNLRI MMEKGDFLSG QGSLTYKDPS EDYIDMICEK IHLSKKLRVG IDCGNGTASL
FAEKLFRRLG VDVYPLYCES DPKFPNHFPD PVKPENLTDL KELVLREKLD LGIGFDGDGD
RIGVVDDKGN IIYGDMLMIL YWREIMPKYP GAVAIIEVKC SQALVDEVKK LGGKPIFYKT
GHSLIKAKMR EIGAVFTGEM SGHMFFADEY YGFDDALYAA ARLLRILSNT DKKLSELLAD
VPKYYSTPEL RVPCPDEEKF DKVEAVKRYF QDKYPIIDVD GARVIFPDGW GLVRSSNTGP
ELIVRCEATS KDGLDKIKNE IQKALLPLKL F
//
