ID A0A1E7ZFT6_9ALTE Unreviewed; 550 AA.
AC A0A1E7ZFT6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:OFC72324.1};
GN ORFNames=BFC18_03450 {ECO:0000313|EMBL:OFC72324.1};
OS Alteromonas confluentis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1656094 {ECO:0000313|EMBL:OFC72324.1, ECO:0000313|Proteomes:UP000175691};
RN [1] {ECO:0000313|EMBL:OFC72324.1, ECO:0000313|Proteomes:UP000175691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42603 {ECO:0000313|EMBL:OFC72324.1,
RC ECO:0000313|Proteomes:UP000175691};
RA Seilhamer J.J.;
RL Submitted (AUG-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}.
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:OFC72324.1}.
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DR EMBL; MDHN01000005; OFC72324.1; -; Genomic_DNA.
DR RefSeq; WP_070123551.1; NZ_MDHN01000005.1.
DR AlphaFoldDB; A0A1E7ZFT6; -.
DR STRING; 1656094.BFC18_03450; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000175691; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR045244; PGM.
DR InterPro; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
DR PANTHER; PTHR22573:SF57; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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 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};
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:UP000175691}.
FT DOMAIN 41..184
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 214..319
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 326..446
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 487..543
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 550 AA; 59084 MW; 50319C1B36B2B699 CRC64;
MALHPHAGEP AAPEQLINVA ELITQYFTFQ PDVSKPAEAV SFGTSGHRGT AANTTFTDVH
IAAICQALAE YREAQGIDGP LYIGKDTHAL SEPAMITAIE VLTANGVEVV IQLADNASRG
YTPTPVISRT IIRYNRQRSE NLADGIVITP SHNPPSDGGF KYNPPHGGPA DGDVTSVIQK
RANALIANGN KDVKRINIQA ARAEGKVQEA DFMEAYIDDL ASVVDMEAIA KAGLKLGTDP
LGGAGVGYWE RIAEKYGLDI TVVNDKVDPQ FGFMRRDKDG KLRMDCSSAY AMAGLIELKD
KFDLAWGNDP DFDRHGIVCP SSGLMNPNHY LAVSINYLYQ HRPNWPTSLK VGKTLVSSSM
IDRVADSLGR ELAEMPVGFK WFVGGLSNGE IAFAGEESAG GIFLQRNGTT WATDKDGFIM
CLLAAEILAV TGKDPGEHYA ALTEKFSAPV YQRVDVAATL EEKQKLSAMD ASVVTSDSLA
GEPITAVQTH APGNNAAIGG VKVSTENGWF AARPSGTEQI YKIYAESFNG ETHLQSLIKE
AEELVAKIIK
//
