ID L9U795_9GAMM Unreviewed; 530 AA.
AC L9U795;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III {ECO:0000313|EMBL:ELY20481.1};
GN ORFNames=HALTITAN_2836 {ECO:0000313|EMBL:ELY20481.1};
OS Halomonas titanicae BH1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1204738 {ECO:0000313|EMBL:ELY20481.1, ECO:0000313|Proteomes:UP000011651};
RN [1] {ECO:0000313|EMBL:ELY20481.1, ECO:0000313|Proteomes:UP000011651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH1 {ECO:0000313|EMBL:ELY20481.1,
RC ECO:0000313|Proteomes:UP000011651};
RX PubMed=23516210;
RA Sanchez-Porro C., de la Haba R.R., Cruz-Hernandez N., Gonzalez J.M.,
RA Reyes-Guirao C., Navarro-Sampedro L., Carballo M., Ventosa A.;
RT "Draft Genome of the Marine Gammaproteobacterium Halomonas titanicae.";
RL Genome Announc. 1:E0008313-E0008313(2013).
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:ELY20481.1}.
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DR EMBL; AOPO01000017; ELY20481.1; -; Genomic_DNA.
DR RefSeq; WP_009288303.1; NZ_AOPO01000017.1.
DR AlphaFoldDB; L9U795; -.
DR PATRIC; fig|1204738.3.peg.4270; -.
DR Proteomes; UP000011651; 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; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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 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}.
FT DOMAIN 22..167
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 196..303
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 306..425
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 470..516
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 530 AA; 57262 MW; A8C01C2022E4E9D4 CRC64;
MESTVKAFYE ERPSANVVGE RVSFGTSGHR GRSIERTFNA SHIYAITQAV VDYRREAGYQ
GPLFLGFDTH ALSRPAWECA LQVLAANKVP VFVEKDHGYT ATPLISQAIL HHNNPHDLAA
PDVALADGLI ITPSHNPPED GGIKYNPHHG GPADTDATGW IELRANAYLL RQLEDIPTVP
VDEAIAHAQE YDFTAHYVAK LGSVVDMAAI QGANLALGAD PMGGTALPVW QAIAAHYDLN
LDVVNTIVDP EFAFMPPDHD GKIRMDCSSP AAMANLLKIK DRFDIAFGND PDADRHGIVD
ASGLMNPNHF LAVCIDYLIT HRPEWAASLK IGKTLVSSSM IDRVVASHQR ELYEVPVGFK
WFVDGLHEGW LAFGGEESAG ASLLTRDGKA WSTDKDGIVL CLLAAEIMAV TGKTPSEYYR
TLTERFGEPF YKRVDTACSP EEKAAFKKLS AESVTEKTLA GDAITAVLVD APGNGTAIGG
IKVTTENGWF AARPSGTESL YKVYAESFKG AQHLDELIGN AQALLAGVLK
//