ID I7L9T8_9CORY Unreviewed; 542 AA.
AC I7L9T8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:CCI84057.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CCI84057.1};
GN Name=pmmB {ECO:0000313|EMBL:CCI84057.1};
GN ORFNames=BN46_1339 {ECO:0000313|EMBL:CCI84057.1}, HMPREF9719_01671
GN {ECO:0000313|EMBL:EJZ81400.1};
OS Corynebacterium otitidis ATCC 51513.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=883169 {ECO:0000313|EMBL:CCI84057.1, ECO:0000313|Proteomes:UP000011016};
RN [1] {ECO:0000313|EMBL:CCI84057.1, ECO:0000313|Proteomes:UP000011016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:CCI84057.1,
RC ECO:0000313|Proteomes:UP000011016};
RX PubMed=23045487; DOI=10.1128/JB.01412-12;
RA Brinkrolf K., Schneider J., Knecht M., Ruckert C., Tauch A.;
RT "Draft Genome Sequence of Turicella otitidis ATCC 51513, Isolated from
RT Middle Ear Fluid from a Child with Otitis Media.";
RL J. Bacteriol. 194:5968-5969(2012).
RN [2] {ECO:0000313|EMBL:EJZ81400.1, ECO:0000313|Proteomes:UP000006078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:EJZ81400.1,
RC ECO:0000313|Proteomes:UP000006078};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Turicella otitidis ATCC 51513.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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:CCI84057.1}.
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DR EMBL; CAJZ01000195; CCI84057.1; -; Genomic_DNA.
DR EMBL; AHAE01000078; EJZ81400.1; -; Genomic_DNA.
DR RefSeq; WP_004601561.1; NZ_JH815195.1.
DR AlphaFoldDB; I7L9T8; -.
DR STRING; 29321.AAV33_05380; -.
DR PATRIC; fig|883169.3.peg.1609; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_2_11; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000006078; Unassembled WGS sequence.
DR Proteomes; UP000011016; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:CCI84057.1};
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:UP000006078}.
FT DOMAIN 48..171
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 214..315
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..430
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 496..534
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 542 AA; 57453 MW; 62E93686091AC05A CRC64;
MSAPDERVLA RARDWAAHDP DPVTRTEIEA LIEARDPELK SRFAGPLTFG TAGLRGRVEG
GESRLNLATV TIASAGLAEW LSSQVDEPSV VVGCDARYGS DAFRKAAAEV FSAAGLTVYL
LPAQLPTPLT AFAVRRLGAD AGVMVTASHN PAGDNGYKVY LGGRVVEVDE ERGVQLVPPA
DEEIAAAIQR APWPDRIPRD GRGLRAVGPE LVSEYLDAAV ATIGEEDRDL EIVLTPVHGV
GGNIALRALN RAGFGSVSVV EEQFAPDPAF PTAPRPNPEE PGVMDLAIAQ AARQGADLVL
ALDPDADRCA CAVPEGDPTD EGSWRRLTGD EVGGLLGERA AKAHEEGALA SSVVSATRLK
DIAERHGLQW RPTLTGFKWI GRTEGLVFGY EEALGYCADP ARVRDKDGIT AALALADLAQ
RRPLTERLAD LDEAYGAVAT GQLSVASESR ERLEEVSARL REALADSVAG SVVAEAHGLD
EGYLGLPPAS GWLVITERGD RVLARPSGTE PKLKCYLEAR AETRPEAEER LAELKSAVSG
LL
//
