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Database: UniProt
Entry: A0A7L4ZDU7_9FLAO
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Original site: A0A7L4ZDU7_9FLAO 
ID   A0A7L4ZDU7_9FLAO        Unreviewed;       462 AA.
AC   A0A7L4ZDU7;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   02-APR-2025, entry version 14.
DE   SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:QHI34948.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:QHI34948.1};
GN   Name=algC {ECO:0000313|EMBL:QHI34948.1};
GN   ORFNames=IMCC3317_02930 {ECO:0000313|EMBL:QHI34948.1};
OS   Kordia antarctica.
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=1218801 {ECO:0000313|EMBL:QHI34948.1, ECO:0000313|Proteomes:UP000464657};
RN   [1] {ECO:0000313|EMBL:QHI34948.1, ECO:0000313|Proteomes:UP000464657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3317 {ECO:0000313|EMBL:QHI34948.1,
RC   ECO:0000313|Proteomes:UP000464657};
RX   PubMed=23606478; DOI=10.1099/ijs.0.052738-0;
RA   Baek K., Choi A., Kang I., Lee K., Cho J.C.;
RT   "Kordia antarctica sp. nov., isolated from Antarctic seawater.";
RL   Int. J. Syst. Evol. Microbiol. 63:3617-3622(2013).
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; CP019288; QHI34948.1; -; Genomic_DNA.
DR   RefSeq; WP_160127727.1; NZ_CP019288.1.
DR   AlphaFoldDB; A0A7L4ZDU7; -.
DR   KEGG; kan:IMCC3317_02930; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000464657; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:TreeGrafter.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:TreeGrafter.
DR   FunFam; 3.30.310.50:FF:000006; Phosphoglucosamine mutase; 1.
DR   FunFam; 3.40.120.10:FF:000020; Phosphoglucosamine mutase; 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; IPR024086; GlmM_arc-type.
DR   InterPro; IPR050060; Phosphoglucosamine_mutase.
DR   NCBIfam; TIGR03990; Arch_GlmM; 1.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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:QHI34948.1};
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:UP000464657}.
FT   DOMAIN          8..141
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          164..263
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          270..375
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          395..454
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   462 AA;  50247 MW;  07858E2C3518A28B CRC64;
     MTLIKSISGI RGTIGGKVGD NLTPIDAVKF ASAYGTWLKN EYNKSKLTVV IGRDARISGA
     MIQSLVVNTL VGLGIDVIDL DLSTTPTVEI AVPLEKADGG IILTASHNPK QWNALKLLNH
     KGEFLNGADG AKILEIAESD AFDFAEVDDL GSVTRNDSYI DIHIDEVLNL ALVDVEAIKQ
     ANFKVVVDGV NSTGGIAIPR LLRALNVEVV ELYCDPTGHF PHNPEPLKEH LTDISELVVK
     EKADLGVVVD PDVDRLAFIC DDGEMFGEEY TLVACADYVL GKTKGNSVSN LSSSRALRDV
     TEKHGGMYQA SAVGEVNVVT LMKKNKAVIG GEGNGGIIYP ESHYGRDSLV GVALFLTHLA
     EKKMTVRELR DSYPSYFMSK NKIQLTPQLD VDGILKAMAE KYANEDVSTI DGVKIDFPTN
     WVHLRKSNTE PIIRIYTEAK SQKEADDLAQ RVINEIKAIT NL
//
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