ID A0A1B1MG36_STRLN Unreviewed; 549 AA.
AC A0A1B1MG36;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phospho-sugar mutase {ECO:0000313|EMBL:QMV09191.1};
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ANS67524.1};
GN ORFNames=GJU35_28465 {ECO:0000313|EMBL:QMV09191.1}, SLCG_3684
GN {ECO:0000313|EMBL:AXG54839.1}, SLINC_5300
GN {ECO:0000313|EMBL:ANS67524.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS67524.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS67524.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS67524.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG54839.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG54839.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV09191.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV09191.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
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; CP016438; ANS67524.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG54839.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV09191.1; -; Genomic_DNA.
DR RefSeq; WP_067438465.1; NZ_CP046024.1.
DR AlphaFoldDB; A0A1B1MG36; -.
DR STRING; 1915.SLINC_5300; -.
DR KEGG; sls:SLINC_5300; -.
DR PATRIC; fig|1915.4.peg.5874; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; 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; 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 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};
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:UP000092598}.
FT DOMAIN 46..182
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 205..307
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 321..428
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 442..515
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 549 AA; 58592 MW; DD3F1CFAB468848F CRC64;
MHDDLIARAK AWLTEDPDAE TRAELAKLID AEDVQELTAR FAGTLQFGTA GLRGELGAGP
MRMNRSVVIR AAAGLAAHLT QQGHTNGLVV IGYDARHKSA DFARDTAAVM TGAGLRAAVL
PRPLPTPVLA YAIRHLGAVA GVEVTASHNP PRDNGYKVYL GDGSQIVPPA DAQIAAEIAA
ITTLNDVPRP TTGWDTLDDA VLDAYLARTD AVLTPTSPRT ARTVYTAMHG VGKDTLLAAF
TRAGFPPPTL VNEQADPDPD FPTVAFPNPE EPGAMDLAFA VARETNPDLI IANDPDADRC
AVAVKEDNEG NEDDAWRMLR GDEVGALLAA HLVARGAQGT FAESIVSSSL LRRIAEKTGL
PYEETLTGFK WIARVEGLRY GYEEALGYCV DPEGVRDKDG ITAALLITEL ASTLKEEGRT
LLDLLDDLAV EHGLHATDQL SVRVEDLSLI TAAMDRLREH PPTHLAGLPI TRADDLTRGT
AQLPPTDGLR YTLDGARVIV RPSGTEPKLK CYLEVVIPVG SHADLPAART RATTLLTTIK
QDLSRAAGI
//
