ID A0A2H1E947_9FLAO Unreviewed; 569 AA.
AC A0A2H1E947;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:SFZ82177.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:SFZ82177.1};
GN Name=pgcA {ECO:0000313|EMBL:SFZ82177.1};
GN ORFNames=MARIT_1478 {ECO:0000313|EMBL:SFZ82177.1};
OS Tenacibaculum maritimum NCIMB 2154.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1349785 {ECO:0000313|EMBL:SFZ82177.1, ECO:0000313|Proteomes:UP000231564};
RN [1] {ECO:0000313|EMBL:SFZ82177.1, ECO:0000313|Proteomes:UP000231564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 2154T {ECO:0000313|EMBL:SFZ82177.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; LT634361; SFZ82177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H1E947; -.
DR STRING; 1349785.GCA_000509405_01965; -.
DR KEGG; tmar:MARIT_1478; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000231564; Chromosome MARIT.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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 Isomerase {ECO:0000313|EMBL:SFZ82177.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000231564}.
FT DOMAIN 44..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 218..305
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 318..437
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 569 AA; 63451 MW; E24B34D33A1D30FA CRC64;
MEKIINNAKQ WLSDTFDAET KNEITQLIAT KSDELADRFY KNLEFGTGGM RGIMGAGTNR
INKYTLGKAT QGLSNYLQQS FPNKELKVAI AYDCRHNSKK YAKLVADVLS ANHIKVFLFK
DLRPTPELSF AVSYLNCDAG IVLTASHNPP EYNGYKVYWN DGGQIVPPQD KGIIDEVNSL
EYADINFNGN DSLISYVGVE MDEAFWEASL ANGTFGVKER ENLKIVFTSL HGTSITLIPE
VLKRAGYSQV HVVKEQEIPN GDFPSVKSPN PEEPEALQMA IDLANEIDAD IVIGTDPDSD
RVGIAVRDLN GNMKLMNGNQ TMSMMTNFLI NEWKKKGKLN GKQFIGSTIV STNLVNEIAK
SYEVETKVGL TGFKWIAKMI KDHPQQEFIG GGEESFGYMV GSFVRDKDAV TSTLLACEIA
ANAKANNSSF YKELLNLYTN HSFYKEHLIA IVKKGMDGAE QIKQIMINLR NTPFTEIDGS
KVKFLCDYQS SIQKNLLTGE EIIMDVPKSN VLIYHTEDGA KIAVRPSGTE PKIKFYFSVK
SPLDSMDNAL EVEQELDAKI QRVIKELKL
//
