ID A0A1Q2SJX8_9GAMM Unreviewed; 466 AA.
AC A0A1Q2SJX8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=TAO_0066 {ECO:0000313|EMBL:BAW79436.1};
OS Candidatus Nitrosoglobus terrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Candidatus Nitrosoglobus.
OX NCBI_TaxID=1630141 {ECO:0000313|EMBL:BAW79436.1, ECO:0000313|Proteomes:UP000243679};
RN [1] {ECO:0000313|EMBL:BAW79436.1, ECO:0000313|Proteomes:UP000243679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAO100 {ECO:0000313|EMBL:BAW79436.1,
RC ECO:0000313|Proteomes:UP000243679};
RX PubMed=28072419; DOI=10.1038/ismej.2016.191;
RA Hayatsu M., Tago K., Uchiyama I., Toyoda A., Wang Y., Shimomura Y.,
RA Okubo T., Kurisu F., Hirono Y., Nonaka K., Akiyama H., Itoh T., Takami H.;
RT "An acid-tolerant ammonia-oxidizing ?-proteobacterium from soil.";
RL ISME J. 11:1130-1141(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP014836; BAW79436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2SJX8; -.
DR KEGG; ntt:TAO_0066; -.
DR Proteomes; UP000243679; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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};
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:UP000243679}.
FT DOMAIN 16..143
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 161..258
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 263..371
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 397..453
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 466 AA; 51427 MW; D6C1D265DA127088 CRC64;
MEEKLPKLDG TIDPTIFKAY DIRGVVGKTL TSKIVYNIGR AVGSEAVSIG QQTIIVGRDG
RLSGTELIQV LIEGLRATGC NVIDIGLVPT PILYFATHHL NTGTGIMLTG SHNPPDYNGM
KIMLGGKTLA LEEIQALRRR IEMSSYAQGV GDLQTLDMVP AYLQQIANDI KLARPLKVVV
DCGNGAAGEV VPQLLRALGN EVIELYCEIN GHFPNHHPDP SQPENLEDLI GKVKATKADL
GLAFDGDGDR LGVVDSEGRI IWPDRQLMLY AIDILSRHPK ATILYDIKCS RHLDRIITQH
GGRSIMYKTG HSLIKAKMKE TGALLAGEMS GHIFFKERWF GFDDALYTGA RLLEILAADP
RSAKEVFASL PDAVSTPELR IEMAEGDHFQ FMERLLNQAE FPQAEITSID GLRVDFEDGW
GLVRSSNTTP CLVLRFEADN VLALERIKEN FRHLMLKVDS SLVFPF
//
