ID A0A0W0GGQ0_9CHLR Unreviewed; 395 AA.
AC A0A0W0GGQ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KTB47707.1};
DE EC=5.4.2.12 {ECO:0000313|EMBL:KTB47707.1};
GN ORFNames=DEALK_05520 {ECO:0000313|EMBL:KTB47707.1};
OS Dehalogenimonas alkenigignens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1217799 {ECO:0000313|EMBL:KTB47707.1, ECO:0000313|Proteomes:UP000053947};
RN [1] {ECO:0000313|EMBL:KTB47707.1, ECO:0000313|Proteomes:UP000053947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP3-3 {ECO:0000313|EMBL:KTB47707.1,
RC ECO:0000313|Proteomes:UP000053947};
RA Key T.A., Richmond D.P., Bowman K.S., Cho Y.-J., Chun J., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Genome sequence of the organohalide-respiring Dehalogenimonas
RT alkenigignens type strain (IP3-3T).";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
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 -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524}.
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:KTB47707.1}.
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DR EMBL; LFDV01000002; KTB47707.1; -; Genomic_DNA.
DR RefSeq; WP_058438443.1; NZ_QEFQ01000003.1.
DR AlphaFoldDB; A0A0W0GGQ0; -.
DR STRING; 1217799.DEALK_05520; -.
DR PATRIC; fig|1217799.6.peg.569; -.
DR OrthoDB; 9804453at2; -.
DR Proteomes; UP000053947; Unassembled WGS sequence.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR NCBIfam; TIGR00306; apgM; 1.
DR NCBIfam; TIGR02535; hyp_Hser_kinase; 1.
DR PANTHER; PTHR31209:SF4; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR PIRSF; PIRSF006392; IPGAM_arch; 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, ECO:0000313|EMBL:KTB47707.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053947}.
FT DOMAIN 1..369
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 395 AA; 42616 MW; B0CE72D26B6A9C09 CRC64;
MKYVVLIIDG ASGWPAEGLG GKTSLEAAKT PNLDQMARRA TVGLAGTVPV GMEPSSACAC
MSVLGYNPKV FYKGRAAIEA RSLEIPIAAD ETVFRANLVT IENGRMADYS AGHIGSNESA
ELIRFLDEKL GTPELSLHPG VGYRHILKLK GRPETLKAAC TPPHDIPGQP VEDYLPRGEG
SDILRNIMAA SAELLKDHPV NRDRIARGEK PATSLWLFWG SGQLPNMPSF KDRYGLSAAI
TSGVDLLRGL GQMQGMDVLC IQGVTDNADN DYAFQMEQAL GALETYDMVV VHVEAPDEAG
HAGDAEGKVK AIEMIDRDMV GRLREYSRDK LRALIMPDHP TPLKIRTHAA EPVPFMIWGS
GVRTSGARRF TEADAKGTGV TVAEAHNIMS MVVRG
//
