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Database: UniProt
Entry: G8PPX2_PSEUV
LinkDB: G8PPX2_PSEUV
Original site: G8PPX2_PSEUV 
ID   G8PPX2_PSEUV            Unreviewed;       512 AA.
AC   G8PPX2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Carbohydrate kinase, FGGY family {ECO:0000313|EMBL:AEV35891.1};
GN   OrderedLocusNames=PSE_1379 {ECO:0000313|EMBL:AEV35891.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV35891.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV35891.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV35891.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
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DR   EMBL; CP003147; AEV35891.1; -; Genomic_DNA.
DR   RefSeq; WP_014284158.1; NC_016642.1.
DR   AlphaFoldDB; G8PPX2; -.
DR   STRING; 911045.PSE_1379; -.
DR   KEGG; psf:PSE_1379; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_4_5; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07779; FGGY_ygcE_like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   PANTHER; PTHR43095; SUGAR KINASE; 1.
DR   PANTHER; PTHR43095:SF5; XYLULOSE KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AEV35891.1};
KW   Transferase {ECO:0000313|EMBL:AEV35891.1}.
FT   DOMAIN          5..251
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          262..454
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   512 AA;  56792 MW;  9B49C86EE88FC0AA CRC64;
     MTETLLAIDC GSQSIRALLF APDGTLISKV QKPITDYRSD NPGWSEIDPV ILWELLGRCC
     RELWDRGADP AAVKAMSVTT QRGTQIAVDE RGIPLRPAIT WMDERIEDQQ KPLPWLWKTI
     FGVAGLSRSI KSVRSECEVN WIAVNQPGIW KKTYKFLQVS GYLNYKLTDL FRDSTGAQVG
     YIPFDYKKQQ WANANHFLWK LFAFKRSQLP ELIEPGKPIG SVSEEAAQHT GLPEGLPVIS
     AAADKACEVV GCGAVDASVG CLSYGTRATA TIHSRKYFEV ERPLPAYAGG IPRMFTPEAS
     VILGYWMVNW FKEEFGHPEQ EKAREIGSPV EVFFDDLLNS TPPGSHGLTL LPKWGRDNGR
     STPVKGAIIG FGDVHTRGHI YRAIIEGITL ELRRGLKRIE RKSGEKIKVL RVSGGGSQSD
     AIMQITADIF GLPTERPHTF ETAGLGAAIA ASVGAGIHPD FTQAMQAMAR QNEVFEPDPK
     TVELYKQLFE EVYLPMPRRL APLNKALRRI TG
//
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