ID A0A1W1VY17_9BACT Unreviewed; 578 AA.
AC A0A1W1VY17;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:SMB98140.1};
GN ORFNames=SAMN00120144_3499 {ECO:0000313|EMBL:SMB98140.1};
OS Hymenobacter roseosalivarius DSM 11622.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=645990 {ECO:0000313|EMBL:SMB98140.1, ECO:0000313|Proteomes:UP000192266};
RN [1] {ECO:0000313|EMBL:SMB98140.1, ECO:0000313|Proteomes:UP000192266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11622 {ECO:0000313|EMBL:SMB98140.1,
RC ECO:0000313|Proteomes:UP000192266};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FWWW01000080; SMB98140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1VY17; -.
DR STRING; 645990.SAMN00120144_3499; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000192266; Unassembled WGS sequence.
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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000192266}.
FT DOMAIN 48..186
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 209..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 324..445
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 578 AA; 63717 MW; 071578D857801FAE CRC64;
MALPSDVQQK INTWLTGDYD AQTQADIQQL LDSNQEDALN DAFYRDLEFG TGGLRGVMGT
GSNRMNRYTL GMATQGLCNY LLESFPAQEI KVAVAHDSRN NSPEFARIAG GIFSANGITV
YLFEALRPTP ELSYTIRHLG CQSGVVITAS HNPKEYNGYK VYWNDGAQVV APHDKNIIRE
VNEIQSVNAV KFQADESRIH LIGGQLDDAY LSEVQKLSIN PEAIKRQHDL KIVFTPIHGT
GITLVPKALE RFGFTNVSVV EAQATPDGNF PTVVSPNPEE KAAMQMALDQ ARQLDADLVI
ATDPDADRVG IAVKNTQGEW VLVNGNQTAA LLTFYLLSAR KNAGKMTEQD FIVYTIVTSE
VLGDIAKAHG VKSYQTLTGF KYIAGLIRDL EGKETYIGGG EESYGFMIGD FVRDKDAVSA
CAMIAEMAAV AKDNGRTLYE EMVQMYATYG LYREDLISLT KKGQRGAEEI QEMMRDLRAQ
PPHTIAGSPV VELRDYQTGI VRNLQNGQET RTGLESSNVL QFLTEDGSKI SARPSGTEPK
IKFYFSVKQP LDSVNEFEQG YEALGGKIAR IIEDMQLK
//
