ID A0A133XK14_9RHOO Unreviewed; 545 AA.
AC A0A133XK14;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KXB31278.1};
GN ORFNames=AT959_06235 {ECO:0000313|EMBL:KXB31278.1};
OS Dechloromonas denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB31278.1, ECO:0000313|Proteomes:UP000070186};
RN [1] {ECO:0000313|EMBL:KXB31278.1, ECO:0000313|Proteomes:UP000070186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB31278.1,
RC ECO:0000313|Proteomes:UP000070186};
RA Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.;
RT "Nitrous oxide reduction kinetics distinguish bacteria harboring typical
RT versus atypical NosZ.";
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:KXB31278.1}.
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DR EMBL; LODL01000013; KXB31278.1; -; Genomic_DNA.
DR RefSeq; WP_066881766.1; NZ_LODL01000013.1.
DR AlphaFoldDB; A0A133XK14; -.
DR STRING; 281362.AT959_06235; -.
DR Proteomes; UP000070186; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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 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};
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:UP000070186}.
FT DOMAIN 38..178
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 209..313
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 320..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 485..539
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 545 AA; 57767 MW; D6FACE56126AA4AB CRC64;
MAHPLAGQPA PLTSLTDIPA LLAAYRTQPD VSQPTQRVAF GTSGHRGSAF NGSFNEAHIL
AITQAVAEYR AQAGIRGPLF LGMDTHALSA PAQQSALEVL AANGVLTHLQ ANGGYTPTPV
ISRAILAHNA DATAERADGI VITPSHNPPQ DGGIKYNPPH GGPADTDVTG WIEQRANALM
ADGNRGVKRQ PYAQALAAPT THAVDLMKPY ISELGSVIDM ESIRRAGLRI GVDPMGGAAV
AYWQPIAEMY GLNIEVVNTA VDPAFAFMSL DHDGKIRMDC SSPYAMAGLV ALKDRFDIAW
GNDADVDRHG IVTPSLGLMN PNHYLAVAIN YLLTHRQHWP RNAAVGKTLV SSGLIDRVVN
GLERRLLEVP VGFKWFSAGL LDGSICFGGE ESAGASFLRR DGTAWTTDKD GIILGLLAAE
ITAVTGRDPG RHYLDLAERY GTPHYLRIDA AASPAEKAAF KQLTGDRVSA ATLAGEAITA
RLTRAAGNDA PIGGLKVTTE NGWFAARPSG TEDIYKIYAE SFKSEAHLQQ LVAEARELVS
AALAG
//
