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Entry: A0A136Q1X7_9FIRM
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Original site: A0A136Q1X7_9FIRM 
ID   A0A136Q1X7_9FIRM        Unreviewed;       511 AA.
AC   A0A136Q1X7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01038};
DE            Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01038};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01038};
DE            Short=iPGM {ECO:0000256|HAMAP-Rule:MF_01038};
DE            EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01038};
GN   Name=gpmI {ECO:0000256|HAMAP-Rule:MF_01038};
GN   ORFNames=HMPREF3293_02761 {ECO:0000313|EMBL:KXK64681.1};
OS   Christensenella minuta.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC   Christensenella.
OX   NCBI_TaxID=626937 {ECO:0000313|EMBL:KXK64681.1, ECO:0000313|Proteomes:UP000070366};
RN   [1] {ECO:0000313|EMBL:KXK64681.1, ECO:0000313|Proteomes:UP000070366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22607 {ECO:0000313|EMBL:KXK64681.1,
RC   ECO:0000313|Proteomes:UP000070366};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038}.
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         ECO:0000256|HAMAP-Rule:MF_01038};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01038};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01038};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798,
CC       ECO:0000256|HAMAP-Rule:MF_01038}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000256|ARBA:ARBA00008819, ECO:0000256|HAMAP-
CC       Rule:MF_01038}.
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:KXK64681.1}.
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DR   EMBL; LSZW01000064; KXK64681.1; -; Genomic_DNA.
DR   RefSeq; WP_066521716.1; NZ_MAIR01000006.1.
DR   AlphaFoldDB; A0A136Q1X7; -.
DR   STRING; 626937.HMPREF3293_02761; -.
DR   KEGG; cmiu:B1H56_08035; -.
DR   PATRIC; fig|626937.4.peg.2720; -.
DR   OrthoDB; 9800863at2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000070366; 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-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01038; GpmI; 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; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001492; IPGAM; 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, ECO:0000256|HAMAP-
KW   Rule:MF_01038};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01038};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01038}; Reference proteome {ECO:0000313|Proteomes:UP000070366}.
FT   DOMAIN          5..498
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          80..295
FT                   /note="BPG-independent PGAM N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06415"
FT   ACT_SITE        60
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-1"
FT   BINDING         10
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         60
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         152..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         259..262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         399
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         403
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         440
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         441
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         459
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
SQ   SEQUENCE   511 AA;  56320 MW;  0B9C531C8ACD03E4 CRC64;
     MAFTALIIMD GFGLTSQTEG NAIYAEGTPN IKKLMEKYPA TQLGASGMSV GLPDGQMGNS
     EVGHLNIGAG RIVYQELTRI TKSIADGDFF SKQEFMDAVK NVKENSSALH LIGLISDGGV
     HSHQEHLYAL LRLAKENGIG DRTYVHCLMD GRDVPPDSGK GFIEQLEAKI EEIGAGKIAT
     VMGRYYAMDR DNRWERVKLA YDAIVKGEGL DAPDAVLAMQ DSYGRKEYDE FVKPTVITEN
     GEPVAKLKAN DSVIFFNFRP DRARELTRSI TQEDFTGFEH EYFPTYFVSM TQYDKTFENI
     HVAYKPQVLQ NTLGEYLAKQ GKKQFRIAET EKYAHVTFFF NGGVEQPNEG EDRVLIPSPK
     VATYDLQPEM SAPEVCAKAV ELIESQKYDV MILNFANCDM VGHTGIFEAA VKAVRAVDEC
     VGKVVDAILK VGGEVLITAD HGNAEIMVDP ETGGPFTAHS TNPVPCILVS QRHQLDKLRT
     GGILADLAPT MLDLMGLPQP IEMEGKSLLE K
//
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