ID A0A0G0GLT6_9BACT Unreviewed; 439 AA.
AC A0A0G0GLT6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
DE Flags: Fragment;
GN ORFNames=US49_C0018G0001 {ECO:0000313|EMBL:KKQ32068.1};
OS candidate division TM6 bacterium GW2011_GWF2_37_49.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619083 {ECO:0000313|EMBL:KKQ32068.1, ECO:0000313|Proteomes:UP000033926};
RN [1] {ECO:0000313|EMBL:KKQ32068.1, ECO:0000313|Proteomes:UP000033926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000256|ARBA:ARBA00000370};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000256|ARBA:ARBA00008819}.
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:KKQ32068.1}.
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DR EMBL; LBTE01000018; KKQ32068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0GLT6; -.
DR PATRIC; fig|1619083.3.peg.1373; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000033926; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF06415; iPGM_N; 2.
DR Pfam; PF01676; Metalloenzyme; 1.
DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..140
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT DOMAIN 151..206
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT DOMAIN 207..412
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKQ32068.1"
SQ SEQUENCE 439 AA; 49347 MW; CA8AD003A3F862AF CRC64;
LHFIGMLSDA GVHSHQSHLF ALLQVVKRQR FKNNVYLHII TDGRDTQPQV AKNYIGQLQR
EIKKIGVNAQ IASVSGRYFA MDRNSNWDRT KKAFLAITKK QGEAFDDPLS AIDVQYEKDV
TDEFIEPVVI KTSNKKAGLV NKILHSEKQS DDMESGTIKP GDGVIFWNFR SERMRQITEL
MLFKRNDIGT SPPENIKVVT LTTYNELLPV SVMYPDEKVK SPLAKILSNN KFSQGHFAET
EKYAHVTYFF DGGNTTPFSG EKWYLIPSPR VATYDLKPEM SASGITAEIL AQNEKNKFDF
IIVNYANADM VGHSGKLDAT IKAVETIDVQ LKKLMEFLPE TYILITADHG NAECMIDEAT
GGPDKNHSVN PVPFIIAHPD FQLKNKQLDN ELQTTGILAD IAPTILQIFN IQKPDEMTGT
SLFDTLKVSP EVENKSEMS
//
