ID D5V3R2_ARCNC Unreviewed; 466 AA.
AC D5V3R2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ADG91773.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:ADG91773.1};
GN OrderedLocusNames=Arnit_0104 {ECO:0000313|EMBL:ADG91773.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG91773.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG91773.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
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; CP001999; ADG91773.1; -; Genomic_DNA.
DR RefSeq; WP_013133918.1; NC_014166.1.
DR AlphaFoldDB; D5V3R2; -.
DR STRING; 572480.Arnit_0104; -.
DR KEGG; ant:Arnit_0104; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_7; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000000939; 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:ADG91773.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000939}.
FT DOMAIN 5..140
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 169..257
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 262..364
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 371..454
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 466 AA; 52756 MW; 898741A48796B42B CRC64;
MINKSIFREY DIRGIVGNEL NEQSSKLIGY YLGLEAIKRT NVQEPVVVIG YDARIHSPEL
FNYLTSGFNK AGCKVLGMGM VATGVNYFAS FQEFDGEKPN ASVMITGSHN PSPYNGFKIT
INNAPFFGDD IYAMGEEIIN NQNMNIKDNE TYKEIDVKSL YKNYMITEFA HLKGMKQKLI
IDCGNGVADT VLTDILDALE LNYDALYCEP DGTFPNHHPD PSEEKNLKDV IEKLKGDYEY
GFAYDGDADR IAFLTKNHNV KGDIMALLFA KTMKNPVIIG EVKCTQIMYD RINENGTAVM
YKTGHSNLKV KLKELNADMA AEVSGHIFFN DRYYGFDDAI YATFRLLELI FNGMDIDKEI
DSLPKVYSTE EIKVETTEEE KFLLMHQIKK NLITVGDDFP KILDIIEVDG VRIVFEQGWG
LVRASNTTPV LVTRFESTDL EVAKLYENKI NELILRSKNE LSNTTN
//
