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Database: UniProt
Entry: M7NYI0_9BACT
LinkDB: M7NYI0_9BACT
Original site: M7NYI0_9BACT 
ID   M7NYI0_9BACT            Unreviewed;       575 AA.
AC   M7NYI0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:EMR03449.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:EMR03449.1};
GN   Name=pgcA {ECO:0000313|EMBL:EMR03449.1};
GN   ORFNames=ADICEAN_01382 {ECO:0000313|EMBL:EMR03449.1};
OS   Cesiribacter andamanensis AMV16.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC   Cesiribacter.
OX   NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR03449.1, ECO:0000313|Proteomes:UP000011910};
RN   [1] {ECO:0000313|EMBL:EMR03449.1, ECO:0000313|Proteomes:UP000011910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMV16 {ECO:0000313|EMBL:EMR03449.1,
RC   ECO:0000313|Proteomes:UP000011910};
RX   PubMed=23682146;
RA   Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT   from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL   Genome Announc. 1:E00240-13(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}.
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:EMR03449.1}.
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DR   EMBL; AODQ01000025; EMR03449.1; -; Genomic_DNA.
DR   RefSeq; WP_009194782.1; NZ_AODQ01000025.1.
DR   AlphaFoldDB; M7NYI0; -.
DR   STRING; 1279009.ADICEAN_01382; -.
DR   PATRIC; fig|1279009.4.peg.1401; -.
DR   eggNOG; COG1109; Bacteria.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000011910; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase 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; 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   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:0000313|EMBL:EMR03449.1};
KW   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011910}.
FT   DOMAIN          45..180
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          206..311
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          321..446
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   575 AA;  64582 MW;  E054CA00D873E650 CRC64;
     MEIKEKAKKW LNSPAVDADT KQQIQQWLDT NNEAELTEAF YKDLEFGTGG LRGIMGVGSN
     RMNKYTLGLA TQGLANYLKK CYPNQPIKVA IAHDSRNNSR FFAETTADIF SANGIQVYLF
     EELRPTPLLS FAIRYLGCQS GVVLTASHNP KEYNGYKAYW SDGAQLVPPH DKNVILEVNK
     LTDISEVNFQ KNPQYISLIG KEVDEAYMRE VLKLSVSPEA IRAQSDLKIV FTPIHGTGIT
     LVPEVLRRMG FGQVHVVQEQ AEPNGNFPTV EYPNPEEAEA LSLGLKKARE LDADLLMGTD
     PDADRVGIAI KNKAGEWQLL NGNQTGALLL YYLLEAWKEK GKLNGRQYIV KTIVTTDLID
     RMAEHYGVDC YNTLTGFKYI AGVLRELEGK QEFIAGGEES YGYLISDFVR DKDAVASCAM
     IAEMAAWARH NGKGLWELLQ EMYQRFGYYQ EILISVTKPG KSGAEEIQKM MQELRQDPPL
     QIAGSPLKQL MDYELGVCRH PQENREDPLD FPRSNVLQFL TEDGSKISAR PSGTEPKIKF
     YVSVNTPVQP GESPSATQER LQDKVRQIVE DMKLK
//
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