ID A0A175RHU8_9MICO Unreviewed; 554 AA.
AC A0A175RHU8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KTR03377.1};
GN ORFNames=NS184_14010 {ECO:0000313|EMBL:KTR03377.1};
OS Curtobacterium luteum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=33881 {ECO:0000313|EMBL:KTR03377.1, ECO:0000313|Proteomes:UP000078252};
RN [1] {ECO:0000313|EMBL:KTR03377.1, ECO:0000313|Proteomes:UP000078252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS184 {ECO:0000313|EMBL:KTR03377.1,
RC ECO:0000313|Proteomes:UP000078252};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTR03377.1}.
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DR EMBL; LDQC01000083; KTR03377.1; -; Genomic_DNA.
DR RefSeq; WP_058726709.1; NZ_LDQC01000083.1.
DR AlphaFoldDB; A0A175RHU8; -.
DR STRING; 33881.NS184_14010; -.
DR PATRIC; fig|33881.3.peg.3268; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000078252; Unassembled WGS sequence.
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; cd05799; PGM2; 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; 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 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}.
FT DOMAIN 54..191
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 215..322
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 331..442
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 499..550
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 554 AA; 57124 MW; 9F5B9545F83E08CA CRC64;
MKLDVDAVVA AGRAWSAQDP DDETRAELDA AVAAAASGDG PAVQELAARF AGRLAFGTAG
LRAELGYGPL RMNRVVVTQA AAGLARFLID SGRSRSVVIG YDGRVNSDVF ARDSAEVMRG
LGLDVTLLPS ALPTPVLAFA VRHLGVGAGV MVTASHNPPR DNGYKVYLGE GDEGSQIVPP
VDATIAAAID AVAAGSIVDL PRATDYTVAG PDLLEAYVAA TAATVPAPAL PAPDQPTVVY
TAMHGVGWET ARAVFERAGY AVPDTVPEQI QPDGAFPTVS FPNPEEPGAM DLAIARGLAA
GADLVIANDP DADRLALAIP DGAGSFRRLS GNEVGWLLGW QAAARAASDR RGGTLAASIV
SSPALARVAE RHGLGYRDTL TGFKWVSRVP DLVFGYEEAL GYLVDPDVVR DKDGISAALA
LLDLATTLAA DGQTIADRLE AFAAEFGAFA SGQVATRVDD LARIGEIMAA LRADPPSSLG
PVAVRSVTDY ADGADGFPPS DILRYDLEGD ARVIVRPSGT EPKVKVYIDT VAGTSAEAQG
LVDALATAVR PLVS
//
