ID R5DU98_9FIRM Unreviewed; 400 AA.
AC R5DU98;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Proposed homoserine kinase {ECO:0000313|EMBL:CCX83733.1};
GN ORFNames=BN798_00196 {ECO:0000313|EMBL:CCX83733.1};
OS Eubacterium sp. CAG:86.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262895 {ECO:0000313|EMBL:CCX83733.1, ECO:0000313|Proteomes:UP000017940};
RN [1] {ECO:0000313|EMBL:CCX83733.1, ECO:0000313|Proteomes:UP000017940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:86 {ECO:0000313|Proteomes:UP000017940};
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:CCX83733.1}.
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DR EMBL; CAXC010000117; CCX83733.1; -; Genomic_DNA.
DR AlphaFoldDB; R5DU98; -.
DR Proteomes; UP000017940; 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; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
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:CCX83733.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017940};
KW Transferase {ECO:0000313|EMBL:CCX83733.1}.
FT DOMAIN 1..371
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 400 AA; 44401 MW; C2A267B5D1A33184 CRC64;
MKYLIILGDG MADKDIPELG GKTPLEYADT PTMDKYSKMS EIGMVHTIPD GMAPGSDTAN
LSVLGYNPRD YYTGRSPLEA LSIGVDMKTT DVALRCNIVT VSTDELPYEE KTIIDHSSSE
ISTEDAAVLL EAVRKELEND IYKFYVGTSY RHLTIWDKGE VVDLTPPHDV LGQKIGQYLP
KDDKLREMMK KSYDILSNHP INVERMKRGL NPANSLWFWG AGTRPMLTSF EEKTGHKGAM
ISAVDLLKGI AVGAGMKVIE VEGANGGLDT NYEGKADAAV DVLLNGGCDF AYIHLEAPDE
MGHQGSYERK VKAIENLDKR IIKRVVEKME AAGEDFRMLV LPDHPTPVAI RTHVSDPVPY
MLYDSTDKKN NTWSYNEKDG EASGNYIAEG HTIINRLFEK
//
