ID R6INZ9_9CLOT Unreviewed; 404 AA.
AC R6INZ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Putative homoserine kinase {ECO:0000313|EMBL:CDB52048.1};
GN ORFNames=BN539_00280 {ECO:0000313|EMBL:CDB52048.1};
OS Clostridium sp. CAG:217.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262779 {ECO:0000313|EMBL:CDB52048.1, ECO:0000313|Proteomes:UP000018364};
RN [1] {ECO:0000313|EMBL:CDB52048.1, ECO:0000313|Proteomes:UP000018364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:217 {ECO:0000313|Proteomes:UP000018364};
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:CDB52048.1}.
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DR EMBL; CBDU010000100; CDB52048.1; -; Genomic_DNA.
DR AlphaFoldDB; R6INZ9; -.
DR STRING; 1262779.BN539_00280; -.
DR Proteomes; UP000018364; 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:CDB52048.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018364};
KW Transferase {ECO:0000313|EMBL:CDB52048.1}.
FT DOMAIN 1..378
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 404 AA; 43881 MW; B8B068692ED6AFBE CRC64;
MKYVVVLCDG MADYPVPALG GKTPMMVAKK PHIDALAAKA EVGLVRTVAP GLKPGSDVAN
MSVLGFDPHR FYTGRSPLEA ASIGIDMKDS DVSLRTNLVT LSDKGEPFAD KVIEDYCADD
ISTEEARQLI EAVQAAFGGG EYDFYTGVSY RHCLIWHGGT TELGNMTPPH DITGKVIGPH
LSTAETARPL LEMMEKSFDL LKDHPVNKAR VAAGRRPANC IWLWGEGKRP ALQPFEALYG
IKGGMVSAVD LLKGIANCAG MEVAEVPGAT GYIDTDFEGK AKAALDLLTR NDLVYVHFEA
PDECGHRNEP ENKVKAIEMI DSRVLPILEE GLEQYEDYKI LLLPDHPTPI VTRTHASDPV
PYLLYQKSAP KTGVDTINEE TAKATGIYME NGPAMMPHFL GQDA
//
