ID B4U966_HYDS0 Unreviewed; 458 AA.
AC B4U966;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ACG57677.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:ACG57677.1};
GN ORFNames=HY04AAS1_0991 {ECO:0000313|EMBL:ACG57677.1};
OS Hydrogenobaculum sp. (strain Y04AAS1).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobaculum.
OX NCBI_TaxID=380749 {ECO:0000313|EMBL:ACG57677.1};
RN [1] {ECO:0000313|EMBL:ACG57677.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y04AAS1 {ECO:0000313|EMBL:ACG57677.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Kiss H., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Resenback A.-L., Mead D.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACG57677.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y04AAS1 {ECO:0000313|EMBL:ACG57677.1};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; CP001130; ACG57677.1; -; Genomic_DNA.
DR AlphaFoldDB; B4U966; -.
DR STRING; 380749.HY04AAS1_0991; -.
DR KEGG; hya:HY04AAS1_0991; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_0; -.
DR OrthoDB; 9806956at2; -.
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; cd05800; PGM_like2; 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; 2.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ACG57677.1};
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}.
FT DOMAIN 2..134
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 151..251
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 260..368
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 400..449
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 458 AA; 51833 MW; 2134EB8629943F97 CRC64;
MIKFGTDGWR AIIGFEFSQD NIVKVAKAHA KALKRHGLNK VIVGYDHRFL GEKFAMLVAD
IMKTDGIEAD ITKGAVSTPN ISFAVKYMGY HQGVMITASH NPYYYNGYKI KESFGGAATP
EFISEVEDEI KNIKDIDFKE HDIKRADIIS QYIEKTLSNI DKNILFEKEL NIVHDSMYGP
AFKYYLEAFK DKKLNLFFIR HHKDALFGEG APEPVEKNLR ILKDKVKTVK ANLGIANDGD
GDRIALVDEN GEFVNSQLVY ILLMLHILKN KGIKKGVVVK TVSTSFLVDR ICKDFGIEVE
ETPVGFKYIN EIVLKKDVIF GGEESGGYGF PFFLPERDGF LSGLFIIEMM LLEDKSLSAI
IKDIFDKYGE AYYNRVDLKV EEHIKDRLKN LIKNPPDTLD GIKVQKVNTK DGLKLIFEDD
SWVMLRASGT EPLIRIYAEA SSKDLLNTLL LKAQKLVS
//
