(data stored in SCRATCH zone)

SWISSPROT: D6ZCQ7_SEGRD

ID   D6ZCQ7_SEGRD            Unreviewed;       408 AA.
AC   D6ZCQ7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 54.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS00041088};
DE            EC=2.7.2.3 {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS00041088};
GN   Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145};
GN   OrderedLocusNames=Srot_0617 {ECO:0000313|EMBL:ADG97099.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97099.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG97099.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + ATP = 3-phospho-D-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216;
CC         EC=2.7.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00145,
CC         ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS01120514};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00145, ECO:0000256|RuleBase:RU000695,
CC       ECO:0000256|SAAS:SAAS00041112}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145,
CC       ECO:0000256|SAAS:SAAS00041091}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145,
CC       ECO:0000256|RuleBase:RU000695, ECO:0000256|SAAS:SAAS00041072}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532,
CC       ECO:0000256|SAAS:SAAS01085159}.
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DR   EMBL; CP001958; ADG97099.1; -; Genomic_DNA.
DR   RefSeq; WP_013137555.1; NC_014168.1.
DR   STRING; 640132.Srot_0617; -.
DR   EnsemblBacteria; ADG97099; ADG97099; Srot_0617.
DR   KEGG; srt:Srot_0617; -.
DR   eggNOG; ENOG4105BZA; Bacteria.
DR   eggNOG; COG0126; LUCA.
DR   HOGENOM; HOG000227107; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   OrthoDB; 462069at2; -.
DR   BioCyc; SROT640132:G1GLH-622-MONOMER; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZCQ7.
DR   SWISS-2DPAGE; D6ZCQ7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|PIRSR:PIRSR000724-2, ECO:0000256|SAAS:SAAS00041066};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|SAAS:SAAS00041081};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|RuleBase:RU000695, ECO:0000256|SAAS:SAAS00041106};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS00041108,
KW   ECO:0000313|EMBL:ADG97099.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|SAAS:SAAS00041094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|RuleBase:RU000532, ECO:0000256|SAAS:SAAS00041076,
KW   ECO:0000313|EMBL:ADG97099.1}.
FT   NP_BIND     359    362       ATP. {ECO:0000256|HAMAP-Rule:MF_00145,
FT                                ECO:0000256|PIRSR:PIRSR000724-2}.
FT   REGION       24     26       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00145, ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   REGION       62     65       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00145, ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING      39     39       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00145, ECO:0000256|PIRSR:PIRSR000724-
FT                                1}.
FT   BINDING     121    121       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00145, ECO:0000256|PIRSR:PIRSR000724-
FT                                1}.
FT   BINDING     161    161       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00145, ECO:0000256|PIRSR:PIRSR000724-
FT                                1}.
FT   BINDING     211    211       ATP. {ECO:0000256|HAMAP-Rule:MF_00145,
FT                                ECO:0000256|PIRSR:PIRSR000724-2}.
FT   BINDING     299    299       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00145}.
FT   BINDING     330    330       ATP. {ECO:0000256|HAMAP-Rule:MF_00145,
FT                                ECO:0000256|PIRSR:PIRSR000724-2}.
SQ   SEQUENCE   408 AA;  42455 MW;  B5D4E886F1E52CC0 CRC64;
     MAISTLDDLL AAGVSGRGVL VRSDLNVPLD GSKITDPGRI AASVPTLKKL AEAGAKVVVA
     AHLGRPDGAP DPKYSLGPVA AELAERLGRH VQLAGDVVGQ DALARSEGLT SGDVLLLENV
     RFDPRETSKD DSARQSLARD LVELVGEDGA FVSDGFGVVH RKQASVYDVA TLLPAYAGDL
     VAAEAAVLRR LTESPERPYA VVLGGSKVSD KLAVIEHLAP RVDTLVIGGG MAFTFLLAQG
     HSVGGSLVQE DQVENAKSLL QRYGSVLKLP LDVVVADTFA ADAQTQTVAA DAIPDGWMGL
     DVGPASHRHF RQALSDAKTI FWNGPLGVFE FPAFAWGTRA LAEAIVEETA KGAFSVVGGG
     DSAAAVRTLK LGEDDFSHIS TGGGASLEFL EGKTLPGIAV LDRSGQER
//

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