ID A0A0C9PBR4_9BACT Unreviewed; 434 AA.
AC A0A0C9PBR4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Phosphoglycerate mutase AP superfamily {ECO:0000313|EMBL:GAN32306.1};
GN ORFNames=BROSI_A0818 {ECO:0000313|EMBL:GAN32306.1};
OS Candidatus Brocadia sinica JPN1.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=1197129 {ECO:0000313|EMBL:GAN32306.1, ECO:0000313|Proteomes:UP000032309};
RN [1] {ECO:0000313|EMBL:GAN32306.1, ECO:0000313|Proteomes:UP000032309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPN1 {ECO:0000313|EMBL:GAN32306.1,
RC ECO:0000313|Proteomes:UP000032309};
RA Oshiki M., Shinyako-Hata K., Satoh H., Okabe S.;
RT "Draft Genome Sequence of an Anaerobic Ammonium-Oxidizing Bacterium,
RT "Candidatus Brocadia sinica".";
RL Genome Announc. 3:e00267-15(2015).
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:GAN32306.1}.
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DR EMBL; BAFN01000001; GAN32306.1; -; Genomic_DNA.
DR RefSeq; WP_052562443.1; NZ_BAFN01000001.1.
DR AlphaFoldDB; A0A0C9PBR4; -.
DR OrthoDB; 9804453at2; -.
DR Proteomes; UP000032309; Unassembled WGS sequence.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:InterPro.
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; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR NCBIfam; TIGR00306; apgM; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000032309}.
FT DOMAIN 2..428
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 434 AA; 47813 MW; AD2861C68C7FF28B CRC64;
MKKILYIVLD GLGDGKYPCK ELGNRTPLEA ASTPAMDMLA REGQSGLMYT VGKDIAPESD
IAVISILGYD AMKYYTGRGP LEALAAGIKI NDGDLAFRAN FATRGTGRSI KDRRVGRNLS
TEEATQLCKE IKKKVKLESV PATFTFKNTL EYRGVLVIRD NNDKLSGYVT NTDPAYIKHG
LLGVAKETGT FENIVEYCMP TRDCPDTEAA YRSALLVNEF TLKSCEVLDQ SEVNKNRIKK
GHLPANLVLL RDAGDHLPKL PSIKSKFKTH FGCFVEMPTE EGIALLTGMK IVPIPPPTKD
LEKDYTLRAN MTIKHMKNYD GLYIHIKGPD VPGHDGDAIR KKAVIEAIDQ YYLTPLINSI
DLDKTIVAIT ADHSTPCRLK SHSDDPVPLL ICGGNIKPDT TRSFSEKTCL AGKIGKIHGT
QLLPLLIKYA NTKK
//
