ID R7BIF8_9FIRM Unreviewed; 402 AA.
AC R7BIF8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Putative homoserine kinase {ECO:0000313|EMBL:CDD64903.1};
GN ORFNames=BN614_00858 {ECO:0000313|EMBL:CDD64903.1};
OS Firmicutes bacterium CAG:341.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263019 {ECO:0000313|EMBL:CDD64903.1, ECO:0000313|Proteomes:UP000018400};
RN [1] {ECO:0000313|EMBL:CDD64903.1, ECO:0000313|Proteomes:UP000018400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:341 {ECO:0000313|Proteomes:UP000018400};
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:CDD64903.1}.
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DR EMBL; CBHK010000095; CDD64903.1; -; Genomic_DNA.
DR AlphaFoldDB; R7BIF8; -.
DR STRING; 1263019.BN614_00858; -.
DR Proteomes; UP000018400; 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:CDD64903.1};
KW Transferase {ECO:0000313|EMBL:CDD64903.1}.
FT DOMAIN 1..400
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 402 AA; 44748 MW; BB85CE5FF4174896 CRC64;
MKYVVVLYDG MADYPVPALG GKTPMMCAKK PNMDFLAKRS EVGLIKTVAD GLKPGSDVAN
MSVLGFDPMK YYTGRSPLEA ASIGIDMKPS DVSLRTNLVT LSEDDLPYEQ KTIEDYCADD
ISTEEAEILI KYIDEKLGTD EFKFYPGVSY RHCLIWNNGT TDLGKMTPPH DITGKVITEY
LSTSENAKPL IELMKKSYDL LKDHPVNIAR KKAGKRPANS IWLWGEGKRP ALSPFEEIYG
IKGAVVSAVD LIKGIGGCAK MEVAEVEGAT GYIDTNFEGK AKAAIDCLER NDLVYVHFEA
PDECGHRNEP ENKVRAIELI DERVLPIIFD GLKKYDDYKI MILPDHPTPI VTRTHASDPV
PYLIYHKQNE IDGVDTINEE TAKETGNFIE NGPSIMKHFL ND
//
