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Database: UniProt
Entry: E6MKU0_9BACT
LinkDB: E6MKU0_9BACT
Original site: E6MKU0_9BACT 
ID   E6MKU0_9BACT            Unreviewed;       409 AA.
AC   E6MKU0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Proposed homoserine kinase {ECO:0000313|EMBL:EFV05750.1};
DE            EC=5.4.2.- {ECO:0000313|EMBL:EFV05750.1};
GN   ORFNames=HMPREF9420_0107 {ECO:0000313|EMBL:EFV05750.1};
OS   Segatella salivae DSM 15606.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=888832 {ECO:0000313|EMBL:EFV05750.1, ECO:0000313|Proteomes:UP000003874};
RN   [1] {ECO:0000313|EMBL:EFV05750.1, ECO:0000313|Proteomes:UP000003874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15606 {ECO:0000313|EMBL:EFV05750.1,
RC   ECO:0000313|Proteomes:UP000003874};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) 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:EFV05750.1}.
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DR   EMBL; AEQO01000010; EFV05750.1; -; Genomic_DNA.
DR   RefSeq; WP_007133401.1; NZ_GL629647.1.
DR   AlphaFoldDB; E6MKU0; -.
DR   STRING; 888832.HMPREF9420_0107; -.
DR   eggNOG; COG3635; Bacteria.
DR   HOGENOM; CLU_034906_2_0_10; -.
DR   OrthoDB; 9804453at2; -.
DR   Proteomes; UP000003874; 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, ECO:0000313|EMBL:EFV05750.1};
KW   Kinase {ECO:0000313|EMBL:EFV05750.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003874};
KW   Transferase {ECO:0000313|EMBL:EFV05750.1}.
FT   DOMAIN          1..390
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   409 AA;  45855 MW;  4700B789374387BC CRC64;
     MKHIIILGDG MADHPVKRLG DKTLLQYANT PYMDLLAKQG RSGMLNTIPE GFLPGSEVAN
     TAILGYDLNK VYEGRGPLEA ASIEYDMQPD DLALRCNIIE IEDECIKNHH GGHLTTEEGD
     MLIQFLNDKL GNEQIKFITG IQYRHLLVIK GGNKHITCAP PHDHPNEEWK SLLVQPEEGY
     HMKDDHRMSP QATANLLNEL IVKSQTLLAN HPFNLHRKAK ANSIWPWSGG YRPSMSTLMQ
     LYPEIKSGSV ISAVDLIRGI GHYAGLDVIK VNGTTGLADT NYEGKVKAAI EALEKQDFVY
     LHIEASDEAG HDGDLDLKLK TIENLDTRVI KPLYETISKW QEPVCIALLP DHPTPVEIRT
     HVKEPVPFVI WHPNILPDNV STYDEVSCRE GGYGMLSLQQ FMETFMKIQ
//
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