ID I0K5J6_9BACT Unreviewed; 494 AA.
AC I0K5J6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:CCG99399.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CCG99399.1};
GN ORFNames=FAES_1389 {ECO:0000313|EMBL:CCG99399.1};
OS Fibrella aestuarina BUZ 2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCG99399.1, ECO:0000313|Proteomes:UP000011058};
RN [1] {ECO:0000313|EMBL:CCG99399.1, ECO:0000313|Proteomes:UP000011058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX PubMed=22689241; DOI=10.1128/JB.00550-12;
RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT Bacterium.";
RL J. Bacteriol. 194:3555-3555(2012).
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; HE796683; CCG99399.1; -; Genomic_DNA.
DR AlphaFoldDB; I0K5J6; -.
DR STRING; 1166018.FAES_1389; -.
DR KEGG; fae:FAES_1389; -.
DR PATRIC; fig|1166018.3.peg.3121; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_10; -.
DR Proteomes; UP000011058; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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, ECO:0000313|EMBL:CCG99399.1};
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:UP000011058}.
FT DOMAIN 28..164
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 190..290
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 297..401
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 425..483
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 494 AA; 53511 MW; 174354DC65BE8371 CRC64;
MADQQTNVPK ADKQQLQPYH VALIKSISGI RGTIGGRTGE SLTPLDVVKF TAAFGQWLLN
GQRGQPGPHT VVIGRDGRLS GPMVSQLVAA TLQGMGLNVL DLGLSTTPTV EMAVPGENAI
GGIILTASHN PIQWNALKLL NSKGEFISGA DGEALLAIAE AESFTFAEVK KLGQYRTDSA
SETSWMQKHI DQILALPLVD REAIVKRNFK VVVDAVNSTG GLAVPMLLTA LGVELITKLH
CEPTGNFAHN PEPLPENLTD ILNATRRDSQ DLGIVVDPDV DRLAFICEDG SPFGEEYTLV
AVADYVLKNS PEGRRNTVSN LSSTIALRDV TQKYGGQHFA SAVGEVNVVE MMKANDALIG
GEGNGGIIYP ELHYGRDALV GIALFLSHLA RFGKSASILR RTYPSYYISK NKIELTPNID
VDAVLDKIKA KYARNPVNTA DGVKIEFDKE WVHLRKSNTE PIIRIYSESD TLSTADYLAN
KIISDIREVI ADKM
//
