ID I3Z864_BELBD Unreviewed; 577 AA.
AC I3Z864;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AFL85432.1};
GN OrderedLocusNames=Belba_2901 {ECO:0000313|EMBL:AFL85432.1};
OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL85432.1, ECO:0000313|Proteomes:UP000006050};
RN [1] {ECO:0000313|Proteomes:UP000006050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC {ECO:0000313|Proteomes:UP000006050};
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Belliella baltica DSM 15883.";
RL Submitted (JUN-2012) 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; CP003281; AFL85432.1; -; Genomic_DNA.
DR RefSeq; WP_014773382.1; NC_018010.1.
DR AlphaFoldDB; I3Z864; -.
DR STRING; 866536.Belba_2901; -.
DR KEGG; bbd:Belba_2901; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_10; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000006050; Chromosome.
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:UP000006050}.
FT DOMAIN 49..187
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 330..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 577 AA; 64284 MW; 45A973837596481E CRC64;
MTNVDPIIIA KAESWLKSNI DEKSKSEIQK LLASEDKTEL IDSFYRDLEF GTGGLRGIMG
VGSNRMNVYT IGMATQGLAN YLLKSFPNEE ISVAITHDCR INNTLFADTT TNVFTANGIK
VYYYREMRPT PMLSFAIRHF GCKSGVMVTA SHNPKEYNGY KAYWEDGGQV VAPHDVNIIS
EVQKITSVDD VNWNKNDALI EYIEADFDLI YLNEVKKLSL SPNEIMLQKD MPIVFSPIHG
ASGRTVPAAL KIYGFENIHI VKEQAEPDGT FPTVIYPNPE EKEALTMAIE LGKKVNAELV
LACDPDGDRY AACIPDGNGG FELLNGNQGG SLITYYLLSK WREHGKLTGD QFMVNTIVTT
ELINAICAGF NVTCYNVLTG FKNIAAIIKQ LEGKQQYIAG GEESYGYMVG DFVRDKDANS
AAAIFAELVA YYKSKGQSIQ DVLAEIYMKY GFYKEHLISV TKKGKDGAEQ IQALMAGFRK
DKPSEINGTK VVKIVDVKES VIYDLLNNKE EKLEMDKSNV IQFYLEDGSK ISARPSGTEP
KIKYYFSVNE KLPNREAYKA VEASLDKKIQ GLMSFFG
//
