GenomeNet

Database: UniProt
Entry: R5KEG6_9BACT
LinkDB: R5KEG6_9BACT
Original site: R5KEG6_9BACT 
ID   R5KEG6_9BACT            Unreviewed;       399 AA.
AC   R5KEG6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Putative homoserine kinase {ECO:0000313|EMBL:CCY65103.1};
GN   ORFNames=BN467_01836 {ECO:0000313|EMBL:CCY65103.1};
OS   Prevotella sp. CAG:1124.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262920 {ECO:0000313|EMBL:CCY65103.1, ECO:0000313|Proteomes:UP000017956};
RN   [1] {ECO:0000313|EMBL:CCY65103.1, ECO:0000313|Proteomes:UP000017956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1124 {ECO:0000313|Proteomes:UP000017956};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCY65103.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAYO010000152; CCY65103.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5KEG6; -.
DR   Proteomes; UP000017956; Unassembled WGS sequence.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; 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};
KW   Kinase {ECO:0000313|EMBL:CCY65103.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017956};
KW   Transferase {ECO:0000313|EMBL:CCY65103.1}.
FT   DOMAIN          12..375
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   399 AA;  44571 MW;  8F721E3328C230B2 CRC64;
     MADHPVARLG GKTLLQYADT PNMDMLARTG RTGRLTTIPD GFQPGSEVAN TAILGYDLNQ
     VYEGRGPLEA ASIGYEMRPD DLALRCNIIT LENGLIKNHH GGHLTTEDSD VLIKHLNKCL
     GNDNIHFITG TQYRHLLIIR NGNKHIECAP PHDHPNEPWR NLMVKPEKGW EELDEDGRMS
     AQETADIINK LIIESQYYLA QKQSQCNEQE CLSIWPWGGG YRPKMKPLSE IYPQVKSGSV
     ISAVDLIRGI GHYAGLRIIK VKGATGLANT NYEGKTQAAL EALRTDDFVF LHIEASDEAG
     HDGNLDLKLK TIENLDKRVV GPIFKEISTW NDTPVCIAVL PDHPTPVEIR THINEPVPFL
     IWYPGIIPDE VQTYNEVSCV SGSYGLLHLN EFIETFIRI
//
DBGET integrated database retrieval system