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
//