ID   D1BK54_SANKS            Unreviewed;       622 AA.
AC   D1BK54;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ACZ22463.1};
GN   OrderedLocusNames=Sked_25590 {ECO:0000313|EMBL:ACZ22463.1};
OS   Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC   Sanguibacter.
OX   NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ22463.1, ECO:0000313|Proteomes:UP000000322};
RN   [1] {ECO:0000313|EMBL:ACZ22463.1, ECO:0000313|Proteomes:UP000000322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC   {ECO:0000313|Proteomes:UP000000322};
RX   PubMed=21304646;
RA   Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA   Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA   Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL   Stand. Genomic Sci. 1:110-118(2009).
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}.
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DR   EMBL; CP001819; ACZ22463.1; -; Genomic_DNA.
DR   RefSeq; WP_012867532.1; NC_013521.1.
DR   AlphaFoldDB; D1BK54; -.
DR   STRING; 446469.Sked_25590; -.
DR   KEGG; ske:Sked_25590; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_2_11; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000000322; 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   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR001763; Rhodanese-like_dom.
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.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          254..317
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   622 AA;  64325 MW;  536DA9C457B6D18F CRC64;
     MTSTESTDST GATATEDLDA LARRVEAWIA DDPDAFSRNE LTALLATARS GEEHVGDAAV
     EDLRDRFAGS LQFGTAGLRG AMQAGPNRMN RAVILRAAAG LAAYLVGSLG DEAGAEGGHK
     HGLLHRHEAA PARPKIVVGY DARHNSHTYA LDSAAVFTAA GLDVVLLPSA LPTPVLAFAV
     RHLDADAGVM VTASHNPPAD NGYKVYLGGR AVTGSGQGAQ IVPPFDALIA AKIAAAPAAA
     QVPRAEDGWS IAGPDVLEAY LASVGRLAVD EAPRDLKIVV TPLHGVGGAV VESVLRGAGY
     HDVFLVPEQA EPDPAFPTVA FPNPEEPGAI DLSLAYAQTL GADLVIANDP DADRCAVAVK
     DHRAVLDHAK NSGGDTGPQE GWRMLHGDEV GALLGELVAS SATSGLLASS IVSSRLLGRI
     ATAHGLDHAS TLTGFKWISR VDGLVFGYEE ALGYCVDPAQ VRDKDGISAA LRMVQLADTL
     KAQGRTLVDA LDDLARAHGL HLTDQLSARF TDLAQIPATM QRLRTAPPAS LAGSAVVETV
     DLSDGVDGLP PTDGLRLLAE DGSRVIVRPS GTEPKVKCYL EVIVPVAGDA SVDEVSEARQ
     VASARLQAIR ADMSAALGIA PA
//