ID A9Q1Z0_BRAHO Unreviewed; 563 AA.
AC A9Q1Z0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Pgm {ECO:0000313|EMBL:ABS12709.1};
DE Flags: Fragment;
GN Name=pgm {ECO:0000313|EMBL:ABS12709.1};
OS Brachyspira hyodysenteriae (Treponema hyodysenteriae).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=159 {ECO:0000313|EMBL:ABS12709.1};
RN [1] {ECO:0000313|EMBL:ABS12709.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WA1 {ECO:0000313|EMBL:ABS12709.1};
RX PubMed=18048921; DOI=10.1099/mic.0.2007/008540-0;
RA Rasback T., Johansson K.E., Jansson D.S., Fellstrom C., Alikhani M.Y.,
RA La T., Dunn D.S., Hampson D.J.;
RT "Development of a multilocus sequence typing scheme for intestinal
RT spirochaetes within the genus Brachyspira.";
RL Microbiology 153:4074-4087(2007).
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; EF488208; ABS12709.1; -; Genomic_DNA.
DR RefSeq; WP_012671773.1; NZ_MKXF01000010.1.
DR AlphaFoldDB; A9Q1Z0; -.
DR GeneID; 63963438; -.
DR PATRIC; fig|159.53.peg.1718; -.
DR OMA; GYCVDPE; -.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 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 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}.
FT DOMAIN 46..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 204..312
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 319..439
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 506..549
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT NON_TER 563
FT /evidence="ECO:0000313|EMBL:ABS12709.1"
SQ SEQUENCE 563 AA; 62845 MW; 1CE9DA4CCB8B1501 CRC64;
MEQEVKARID SWLNGSYDEE TKKEIKALLD AGNEKELIDA FYRDLEFGTG GLRGIMGVGT
NRMNKYTVGV ATQGLANYIL KQGGSNYKVA IGYDSRNNSD VFSKAAAEIL SSNGISVYLY
DDIHPISLLS YAVRSLGCIA GIVVTASHNP KEYNGYKVYW TDGAQVIPPH DKNIIDEVLK
VKPEEVKMGD SSKVTIIGKD IEDKYMNDLM GYLVNPDIIK KHHDIKIVYT PIHGSGYKMV
PMALRKAGFT NLTTMEGAQP PNGNFPTVES PNPENPEALK IAVDKAKEIG AELVMGTDPD
CDRMGCALLT KDGSYMYLTG NQIGSIMAYY LITNKKNVKN PFIVKTIVTT ELARAIADAN
NVKIYDVLTG FKWIADVIER DKEGTYLFGF EESFGYCINS NVRDKDGVSS CLMLAEVLAY
CKDNNMTLAD YLESIYEKYG YFYEETISIT KKGADGAKAI ADLMTYYRNN LPKEISGVKV
ESISDYEKKE VYDNTGKKIK DITLPKSNVL QYILEDKTKI TIRPSGTEPK IKFYFEVCVK
ESKDKRLAVA KDKVANFKKF IKE
//
