ID H2CA29_9LEPT Unreviewed; 557 AA.
AC H2CA29;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
GN ORFNames=Lepil_0448 {ECO:0000313|EMBL:EHQ05153.1};
OS Leptonema illini DSM 21528.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptonema.
OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ05153.1, ECO:0000313|Proteomes:UP000005737};
RN [1] {ECO:0000313|EMBL:EHQ05153.1, ECO:0000313|Proteomes:UP000005737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ05153.1,
RC ECO:0000313|Proteomes:UP000005737};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; JH597773; EHQ05153.1; -; Genomic_DNA.
DR AlphaFoldDB; H2CA29; -.
DR STRING; 183.GCA_002009735_00043; -.
DR HOGENOM; CLU_026099_3_1_12; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000005737; 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; 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};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EHQ05153.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR001492-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001492-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005737}.
FT DOMAIN 15..544
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 100..325
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT ACT_SITE 78
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-1"
FT BINDING 22
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 174..175
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 289..292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 432
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 474
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 504
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
SQ SEQUENCE 557 AA; 59767 MW; 30CF1A26AA01CFC3 CRC64;
MKLSLNRTGR SVSGPVVLVI MDGVGLYKGR AEGYPGNAVD LAGAPFLKDQ LQHAPIRLQL
KAHGTAVGMP SDEDMGNSEV GHNALGAGRI FDQGAKLVAG AIASGQLFTG SAWMDLVGSR
ENPGAAVKGA TLHFIGLLSD GNVHSHIDHL IAMLRKAHEA GVRQVRLHIL LDGRDVDETS
ALLYVDKLEA VLKELDATGK NYRIASGGGR MKVTMDRYEA DWSMVELGWK THVAGEGRQF
ASAKEAIETF RNEIPGVTDQ DLPAFVIGES GAPVGQIKDG DAVIFFNFRG DRAIEISRAF
VESDFNVFER HPKVSVKYAG MMQYDGDLKM PPVFLVDPPA IDETLTEYLV AAGVKQYALS
ETQKFGHVTY FWNGNNSAKI SEALETWEEI PSDVISFDRK PRMKADEIGA ALVKAIESGE
YGFLRVNFAN GDMVGHTGIL DAAVAAVEAV DQNLPRILEA VNKKGGILLV TADHGNCEQM
YEVNKKTGEP LKNDKGGFAS KTSHTLNPVP FLVLGNVDGL EASGVAGAGL ANVAATVMTL
LGFEPPAGYL PSVLRWK
//
