ID A4YPH4_BRASO Unreviewed; 546 AA.
AC A4YPH4;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:CAL75800.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:CAL75800.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CAL75800.1};
GN Name=pgm {ECO:0000313|EMBL:CAL75800.1};
GN OrderedLocusNames=BRADO1937 {ECO:0000313|EMBL:CAL75800.1};
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL75800.1, ECO:0000313|Proteomes:UP000001994};
RN [1] {ECO:0000313|EMBL:CAL75800.1, ECO:0000313|Proteomes:UP000001994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(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; CU234118; CAL75800.1; -; Genomic_DNA.
DR RefSeq; WP_011925026.1; NC_009445.1.
DR AlphaFoldDB; A4YPH4; -.
DR STRING; 114615.BRADO1937; -.
DR KEGG; bra:BRADO1937; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_016950_8_1_5; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000001994; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:CAL75800.1};
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:UP000001994}.
FT DOMAIN 41..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 212..319
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 323..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 496..542
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 546 AA; 58463 MW; 6589D2AA252F435B CRC64;
MAKTDPAAGK PIANAALANI PRLITAYYAL KPDPHEPTQR VAFGTSGHRG SSLKTGFNEN
HILATTQALC DYRRQQGLDG PLFVGIDTHA LAEPALASAL EVFGANGVEV MVDKDGGYTP
TPVISHAIIS YNKGRTAHLA DGVVITPSHN PPEDGGYKYN PPHGGPADTD ATAEIERQAN
VYLANDLDGV SRISYAQAKQ RGSVHPHDYI TPYVADLANT VDLDAVKSAG IKIGIDPLGG
AAIAYWAPII ERYGLSATIV NDLVDPTFRF MTADWDGKIR MDCSSPYAMA SLIGMRERFD
VAFANDTDAD RHGIVTRSGG LMNPNHYLAT AIAYLFAHRP DWRSDAAIGK TIVSSSLIDR
VAQKLGRKLV ETPVGFKWFV EGLGSGSFGF AGEESAGASF LKRDGTVWTT DKDGLILGLL
AAEIMAKRGR DPSELYKELA SELGAPVYER IDVPASPPQK AALKALTPEK LGLKELAGDP
VRVIHTKAPG NGQSFGGIKV ETEYGWFAAR PSGTEDVNKL YAESFRDAEH LKRIQSEAQA
ALAKVA
//
