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Database: UniProt
Entry: A0A0D1D733_9RHOB
LinkDB: A0A0D1D733_9RHOB
Original site: A0A0D1D733_9RHOB 
ID   A0A0D1D733_9RHOB        Unreviewed;       496 AA.
AC   A0A0D1D733;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=AlgC protein {ECO:0000313|EMBL:KIT15753.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:KIT15753.1};
GN   Name=algC {ECO:0000313|EMBL:KIT15753.1};
GN   ORFNames=jaqu_24940 {ECO:0000313|EMBL:KIT15753.1};
OS   Jannaschia aquimarina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT15753.1, ECO:0000313|Proteomes:UP000032232};
RN   [1] {ECO:0000313|EMBL:KIT15753.1, ECO:0000313|Proteomes:UP000032232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT15753.1,
RC   ECO:0000313|Proteomes:UP000032232};
RA   Voget S., Daniel R.;
RT   "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT   Roseobacter clade.";
RL   Submitted (FEB-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}.
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:KIT15753.1}.
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DR   EMBL; JYFE01000044; KIT15753.1; -; Genomic_DNA.
DR   RefSeq; WP_043919297.1; NZ_JYFE01000044.1.
DR   AlphaFoldDB; A0A0D1D733; -.
DR   STRING; 935700.jaqu_24940; -.
DR   PATRIC; fig|935700.4.peg.2572; -.
DR   Proteomes; UP000032232; 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:KIT15753.1};
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:UP000032232}.
FT   DOMAIN          24..153
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..389
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          432..484
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   496 AA;  54180 MW;  2B54EFB3E091B634 CRC64;
     MKPQTDVTPN TWAFLRDPMI APTGFREYDA RWKYPDAINL PGVTALGLGL GTQMHARGIE
     PRIAVGNDYR DYSLAIKQAL ILGLTQAGVH VQDIGPAITP MAYFSQFHLD APAVAMVTAS
     HNPNGWTGVK MGFQRPLTHG PDEMAELRDI VLQGRGEARD GGRWERVDGV MEAYLDDLVG
     DFRMSRPLKV VCAAGNGTAA AYGPEVLRRI GVEVVESHCE LDYTFPHYNP NPEAMEMLHD
     MADSVRASGA DLALGFDGDG DRCGVVDDEG EEIFADKVGV IMARDLSALH PGSTFVADVK
     STGLFASDPV LKENGAKADY WKTGHSHMKR RVHEIGALAG FEKSGHYFLA EPVGRGYDDG
     MRVAVEICKL MDRNPDKSMS DLRKALPTVY NTPTLSPHCP DEEKYDTLQR IVDRIVPMKG
     EGSLGGQKIV DVVTVNGARV MLENGGWGLV RASSNTPNLV VVCESPTSKE ELRAIFDDLD
     AIIRHEPNVG DYDQAF
//
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