ID A0A175XZ02_9SPHN Unreviewed; 455 AA.
AC A0A175XZ02;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KZB93692.1};
GN ORFNames=AVM11_11160 {ECO:0000313|EMBL:KZB93692.1};
OS Sphingomonas melonis TY.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=621456 {ECO:0000313|EMBL:KZB93692.1, ECO:0000313|Proteomes:UP000078460};
RN [1] {ECO:0000313|EMBL:KZB93692.1, ECO:0000313|Proteomes:UP000078460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TY {ECO:0000313|EMBL:KZB93692.1,
RC ECO:0000313|Proteomes:UP000078460};
RA Wang H., Zhu P.;
RT "Sphingomonas melonis TY, whole genome shotgun sequencing.";
RL Submitted (MAR-2016) 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:KZB93692.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQCK02000067; KZB93692.1; -; Genomic_DNA.
DR RefSeq; WP_017977318.1; NZ_LQCK02000067.1.
DR AlphaFoldDB; A0A175XZ02; -.
DR STRING; 621456.BJP26_04415; -.
DR GeneID; 67489425; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000078460; 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; 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};
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 10..119
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 166..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 254..363
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 384..447
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 455 AA; 47438 MW; 7038BC4CC9026A58 CRC64;
MSHVLSPTIL REYDIRGTVG RNLAPADATA IGRSFATRIR AAGGTRVAVG RDGRLSSPDL
ETALVAGLVA GGVDVVRIGL GPTPMLYFAE ATLGVDAGIH VTGSHNPRDD NGFKMVLGHR
SFYGADVVDL ARLAATGAWS EGTGSVTHHD VLPAYVARLL AGYAGGAFRI GWDCGNGAAG
PAVERLVAQL PGEHHLLHTL VDGRFPNHHP DPTEEANLAD LKALVREKGL DFGIAFDGDG
DRIGAVDGKG RVLWGDQLLG LLIAPVLAAC PGATVVADVK SSAYVFDRIA ELGGIAVMGA
TGHSPMKEAM LAHAAPIAGE LSGHIFFGHE WYGFDDALYA AVQLIGAVHG SGQSLTTLHD
AMPPFVSTPD LRFAIDPARK AGVIDAVRAR VEATRTPVVA IDGVRVTTAA GWWLLRASNT
QDMLTLRAEA RSQAALDALL AEVDAHLAAC GIARD
//
