(data stored in ACNUC7421 zone)

SWISSPROT: A4ATG7_MARSH

ID   A4ATG7_MARSH            Unreviewed;       514 AA.
AC   A4ATG7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01038};
DE            Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01038};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01038};
DE            Short=iPGM {ECO:0000256|HAMAP-Rule:MF_01038};
DE            EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01038};
GN   Name=gpmI {ECO:0000256|HAMAP-Rule:MF_01038};
GN   OrderedLocusNames=FB2170_16671 {ECO:0000313|EMBL:EAR00737.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00737.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00737.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038,
CC       ECO:0000256|SAAS:SAAS00978404}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = 3-phospho-D-glycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.12; Evidence={ECO:0000256|HAMAP-Rule:MF_01038,
CC         ECO:0000256|SAAS:SAAS01115646};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01038};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01038};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
CC       Rule:MF_01038, ECO:0000256|SAAS:SAAS00850947}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01038,
CC       ECO:0000256|SAAS:SAAS00850933}.
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DR   EMBL; CP002157; EAR00737.1; -; Genomic_DNA.
DR   STRING; 313603.FB2170_16671; -.
DR   EnsemblBacteria; EAR00737; EAR00737; FB2170_16671.
DR   KEGG; fbc:FB2170_16671; -.
DR   eggNOG; ENOG4105CJI; Bacteria.
DR   eggNOG; COG0696; LUCA.
DR   HOGENOM; HOG000223664; -.
DR   KO; K15633; -.
DR   OMA; FMDGRDT; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd16010; iPGM; 1.
DR   Gene3D; 3.40.1450.10; -; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   HAMAP; MF_01038; GpmI; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR011258; BPG-indep_PGM_N.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR036646; PGAM_B_sf.
DR   InterPro; IPR005995; Pgm_bpd_ind.
DR   PANTHER; PTHR31637; PTHR31637; 1.
DR   Pfam; PF06415; iPGM_N; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001492; IPGAM; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   SUPFAM; SSF64158; SSF64158; 1.
DR   TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATG7.
DR   SWISS-2DPAGE; A4ATG7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00850939};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00850936};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00241368};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00241382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   DOMAIN       17    503       Metalloenzyme. {ECO:0000259|Pfam:
FT                                PF01676}.
FT   DOMAIN       95    304       iPGM_N. {ECO:0000259|Pfam:PF06415}.
FT   REGION      166    167       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01038}.
FT   REGION      268    271       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01038}.
FT   ACT_SITE     75     75       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01038}.
FT   METAL        25     25       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL        75     75       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       408    408       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       412    412       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       449    449       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       450    450       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       467    467       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     197    197       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     203    203       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     341    341       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
SQ   SEQUENCE   514 AA;  56569 MW;  4A041F3BA9BF7C95 CRC64;
     MALGSIFALL NNVTMNKKVI LMILDGWGTS PDPKVSAIDN AKTPYIDALY SKYPNAALRT
     DGLNVGLPDG QMGNSEVGHM NLGAGRIVYQ ELTRINLAIE NNTLKDEKVL VDAFDYAKAN
     NKKVHFLGLL SNGGVHSHIN HLKGLLSAAK DNNLDNVYVH AFTDGRDVDP KSGASFVADL
     EDHMAKTTGK IATVTGRYYA MDRDNRWERV KLAYDVIVNG DGQLTDNVVN SLKSSYANDV
     TDEFIKPLVA DKNGIVEEDD VIIFFNFRTD RGRELTNMLS QNDFPEDNTK KLSLHYVTMT
     NYDDSFKGIN VIFNKDNITE TIGEVLSKAG KKQIRIAETE KYPHVTFFFS GGQEEPFEGE
     SRILRNSPKV ATYDLKPEMS AYELRDALVE DLKKQEADFV CLNFANGDMV GHTGIMEAAI
     KACEAVDICV KDVVETGLEN GYSTLLIADH GNCETMINPD GSPHTAHTTN PVPVILIDKN
     LKEIKDGVLG DVAPTILELI GIEQPKAMTG KSLI
//

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