ID C4GJ71_9NEIS Unreviewed; 550 AA.
AC C4GJ71;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II {ECO:0000313|EMBL:EEP67843.1};
GN ORFNames=GCWU000324_02093 {ECO:0000313|EMBL:EEP67843.1};
OS Kingella oralis ATCC 51147.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=629741 {ECO:0000313|EMBL:EEP67843.1, ECO:0000313|Proteomes:UP000003009};
RN [1] {ECO:0000313|EMBL:EEP67843.1, ECO:0000313|Proteomes:UP000003009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51147 {ECO:0000313|EMBL:EEP67843.1,
RC ECO:0000313|Proteomes:UP000003009};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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:EEP67843.1}.
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DR EMBL; ACJW02000003; EEP67843.1; -; Genomic_DNA.
DR RefSeq; WP_003797045.1; NZ_GG665872.1.
DR AlphaFoldDB; C4GJ71; -.
DR STRING; 629741.GCWU000324_02093; -.
DR GeneID; 84905961; -.
DR HOGENOM; CLU_016950_0_2_4; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000003009; 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 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:UP000003009}.
FT DOMAIN 49..190
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 212..316
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 323..427
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 474..535
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 550 AA; 59269 MW; B63DD8CADBF78188 CRC64;
MTYLAQAQNW LAQDPDPETR AELEALIPAA QAGDAAALAE LEARFNGRLQ FGTAGLRGKQ
QAGSMGMNRV LVAQAAKGLA DYILQFDPQN PSIVIGYDGR KNSDIYARDT AEIMAGAGIQ
TRLLPRTLPT PVLAYAIQHF DTSAGVMVTA SHNPPADNGY KVYLGKSNGG GQIVSPADEQ
IAALIDQATQ TPINQYPRSS DYETLGEAVI EAYIAKTAAL AQEPECSLNY VYTAMHGVGK
EVLLKTLAAA KLPLPHIVAE QAEPDPTFHT VAFPNPEEKG ALDLAIALAK KENAEFIIAN
DPDADRLAVA IPDEQGNWKS LHGNVVGCYL GWYLAQKNQG KTGTLACSLV SSPALAQIAQ
KYGFANEETL TGFKYIAKAP NLLYGFEEAL GYLVDPDKVR DKDGISAAIV FLDLVRSLKA
QSKTLLDHAR DFAQTFGAYT SGQISIRVSD LADIGKLMSA LRQNPPSQIG GHAVEQTIDH
LQTERQNDIL VYHLTNGSRL IVRPSGTEPK VKFYLDAKGS SEADAQNVLQ AFDAAVRELL
RQDVYGKQNC
//