ID B3E262_GEOLS Unreviewed; 616 AA.
AC B3E262;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 01-MAY-2013, entry version 33.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE Short=PEP carboxykinase;
DE Short=PEPCK;
DE EC=4.1.1.32;
DE AltName: Full=Phosphoenolpyruvate carboxylase;
GN Name=pckG; OrderedLocusNames=Glov_3462;
OS Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=398767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L.,
RA Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y.,
RA Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.;
RT "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC pathway that produces glucose from lactate and other precursors
CC derived from the citric acid cycle (By similarity).
CC -!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate
CC + CO(2).
CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family.
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DR EMBL; CP001089; ACD97165.1; -; Genomic_DNA.
DR RefSeq; YP_001953685.1; NC_010814.1.
DR STRING; 398767.Glov_3462; -.
DR EnsemblBacteria; ACD97165; ACD97165; Glov_3462.
DR GeneID; 6368947; -.
DR KEGG; glo:Glov_3462; -.
DR PATRIC; 21998591; VBIGeoLov31523_3384.
DR eggNOG; COG1274; -.
DR HOGENOM; HOG000191700; -.
DR KO; K01596; -.
DR OMA; WMRFGED; -.
DR ProtClustDB; PRK04210; -.
DR BioCyc; GLOV398767:GH32-3594-MONOMER; -.
DR UniPathway; UPA00138; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:HAMAP.
DR GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 2.
DR HAMAP; MF_00452; PEPCK_GTP; 1; -.
DR InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008209; PEP_carboxykinase_GTP.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR PANTHER; PTHR11561; PTHR11561; 1.
DR Pfam; PF00821; PEPCK; 1.
DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR SUPFAM; SSF68923; PEP_carboxykinase_N; 1.
DR PROSITE; PS00505; PEPCK_GTP; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW GTP-binding; Kinase; Lyase; Manganese; Metal-binding;
KW Nucleotide-binding; Pyruvate.
FT NP_BIND 262 267 GTP (By similarity).
FT NP_BIND 506 509 GTP (By similarity).
FT REGION 380 382 Substrate binding (By similarity).
FT ACT_SITE 263 263 By similarity.
FT METAL 219 219 Manganese (By similarity).
FT METAL 239 239 Manganese (By similarity).
FT METAL 290 290 Manganese (By similarity).
FT BINDING 72 72 Substrate (By similarity).
FT BINDING 212 212 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 219 219 Substrate (By similarity).
FT BINDING 261 261 Substrate (By similarity).
FT BINDING 382 382 GTP (By similarity).
FT BINDING 413 413 GTP (By similarity).
SQ SEQUENCE 616 AA; 69354 MW; 63C63D9F8456221F CRC64;
MSYEVKNEQL KAWVAEVEAM CEPANIHWCD GSQEEYDRLC GQMVESGTFR KLNPEKRPNS
YLAFSDPIDV ARVEDRTFIC SLNKQDAGPT NNWVAPKEMK ETLKGLFKGC MKGRTMYVIP
FSMGPLGSNI AKIGVEITDS PYVVVNMRIM TRMGKQVLDV LGNGEFVPCL HSVGMPLAEG
QKDVAWPCNK EKYIVHFPEE RAIWSFGSGY GGNALLGKKC LALRIASVQA RDEGWLAEHM
LILGVESPTG EKSYVGAAFP SACGKTNFAM LIPPKPFQDK GWKVTTIGDD IAWIKPGADG
QVYAINPEYG YFGVAPGTNY KTNPNAMISC EKNSIFTNVA LTEDGDVWWE GMDGEVPAKL
TDWQGNAWTP DCGRPAAHPN ARFTAPASQC PCIDPEWENP KGVPMSAFIF GGRRKDTVPL
VYQAFNWNYG VYLASTLGSE TTAAAVGATG NVRRDPFAML PFCGYHMADY FAHWLQFGRS
IARPPRIFSV NWFRKDANGK FIWPGYGENM RVLKWIAERV QGKTGSVECP LGWMPRYEDM
DWEGIEMSRE KFNELMSVDR DVWQNEVISH EELFVKMYDK LPKEFLHIRE LILSSLWRSP
EHWEQIGEVH PEGWNE
//
