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Database: UniProt
Entry: A0A0M7BCY8_9RHOB
LinkDB: A0A0M7BCY8_9RHOB
Original site: A0A0M7BCY8_9RHOB 
ID   A0A0M7BCY8_9RHOB        Unreviewed;       496 AA.
AC   A0A0M7BCY8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:CUH39672.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:CUH39672.1};
GN   Name=algC {ECO:0000313|EMBL:CUH39672.1};
GN   ORFNames=JSE7799_02399 {ECO:0000313|EMBL:CUH39672.1};
OS   Jannaschia seosinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH39672.1, ECO:0000313|Proteomes:UP000049455};
RN   [1] {ECO:0000313|EMBL:CUH39672.1, ECO:0000313|Proteomes:UP000049455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH39672.1,
RC   ECO:0000313|Proteomes:UP000049455};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) 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}.
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DR   EMBL; CYPR01000160; CUH39672.1; -; Genomic_DNA.
DR   RefSeq; WP_055663823.1; NZ_CYPR01000160.1.
DR   AlphaFoldDB; A0A0M7BCY8; -.
DR   STRING; 313367.JSE7799_02399; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000049455; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CUH39672.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049455}.
FT   DOMAIN          24..151
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          172..270
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          276..387
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          430..484
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   496 AA;  54362 MW;  0217DBA24EEF89E8 CRC64;
     MKPLADVSPN TWAFLRDPMI APTGFREYDA RWQYPEGINL PGVTALGLGL GTQMHRRRIE
     PRIAVANDYR DYSLSIKNAL ILGLVQAGIH VQDIGPALSP MAYFSQFHLD APAVAMVTAS
     HNPNGWTGVK MGFERPLTHG PEEMGELRDI VLGGEGEARE GGRWERVDGV MEAYLDDLTG
     DFKMSRKLKV VCATGNGTAS AFAPEVLRRI GVEVVPSHNE LDYTFPHYNP NPEAMEMLHD
     MADSVRASGA DLALGFDGDG DRCGVVDDEG EEIFADIMGV IMARDLSAIH KGATFVADVK
     STGLFASDPV LQANGAKADY WKTGHSHMKR RVHEIGALAG FEKSGHYFLA EPIGRGFDCG
     MRVAVEICKL LDRNPDQSMS DLRRALPKVW NTPTLSPHCP DEEKYETLQR IVDRLVPMKG
     EGTLGGQRIV DVVTVNGARV MLENGGWGLV RASSNTPNLV VVCESPTSKE ELRAIFEDLD
     AVIRQEPNVG DYDQTF
//
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