ID A6QBM2_SULNB Unreviewed; 474 AA.
AC A6QBM2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:BAF72881.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:BAF72881.1};
GN Name=cpsG {ECO:0000313|EMBL:BAF72881.1};
GN OrderedLocusNames=SUN_1934 {ECO:0000313|EMBL:BAF72881.1};
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum.
OX NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF72881.1, ECO:0000313|Proteomes:UP000006378};
RN [1] {ECO:0000313|EMBL:BAF72881.1, ECO:0000313|Proteomes:UP000006378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF72881.1,
RC ECO:0000313|Proteomes:UP000006378};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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}.
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DR EMBL; AP009179; BAF72881.1; -; Genomic_DNA.
DR RefSeq; WP_012083702.1; NC_009663.1.
DR AlphaFoldDB; A6QBM2; -.
DR STRING; 387093.SUN_1934; -.
DR KEGG; sun:SUN_1934; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_7; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000006378; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase 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; IPR016066; A-D-PHexomutase_CS.
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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAF72881.1};
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 6..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 172..268
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 274..378
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 384..467
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 474 AA; 52975 MW; BBE0A4A9899F8F98 CRC64;
MPINKSIFRE YDIRGIYNKE LNEQSVKLIG YHLGQKIGKG KAVSIGYDAR SHSPVLRDYL
TSGLNAAGCT VLDMGMVATP VNYFSNYQKI EDLNPKTPHS SLLTPHLEAS PDTSIMITGS
HNPSEYNGFK ITLDKTPFFG EDIYTLGDAI IADQARIVPD DTEKIDIDVK TPYINFMIKE
FSHLKGLDKK IVIDCGNGVA DTVITDIFDA LQFNYTGLYC EPDGTFPNHH PDPSVEKNLA
DVKAALKKEG DIAFAYDGDA DRIAVLTHKH NIKGDQMALL YAMKMENPTV IGEVKCSQVM
YDELERRGAK AIMYKTGHSN LKVKMKETNA DLACEVSGHI FFKNRYFGYD DAIYATLRML
ELIAEGIDLD KEIEALPTVY STEELNVETT EEEKFAIIDK VKELLINPPA DFPVIKSIID
VDGVRINFDK GWGLVRASNT TPVLVTRFES TDETLAKEYE EKVNQLIESA KVLL
//
