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Database: UniProt
Entry: E1QH32_DESB2
LinkDB: E1QH32_DESB2
Original site: E1QH32_DESB2 
ID   E1QH32_DESB2            Unreviewed;       525 AA.
AC   E1QH32;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Carbohydrate kinase, FGGY {ECO:0000313|EMBL:ADK84875.1};
GN   OrderedLocusNames=Deba_1507 {ECO:0000313|EMBL:ADK84875.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK84875.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK84875.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
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DR   EMBL; CP002085; ADK84875.1; -; Genomic_DNA.
DR   RefSeq; WP_013258328.1; NC_014365.1.
DR   AlphaFoldDB; E1QH32; -.
DR   STRING; 644282.Deba_1507; -.
DR   KEGG; dbr:Deba_1507; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_4_7; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000009047; 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:ADK84875.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW   Transferase {ECO:0000313|EMBL:ADK84875.1}.
FT   DOMAIN          7..255
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          266..458
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   525 AA;  57833 MW;  57BD578BE31B608F CRC64;
     MSEEHNVLAI DVGTQSARAF VFGADGAMID GARAVYDQPY HSPQPGWAEQ DPRMYWDKLA
     EACHGLWRRD LARPESLAAV AVTTQRNTVV CLDAQARPLR PAIVWLDQRR ASDLRHLSRL
     WRALFGVAGL GGTIDYLMAE AEANWLRQHQ PEIWRDTAHY LFLSGYINHK LTGRFADSTA
     CTVGYMPFDY KAQRWAGDLS WKWSAIPVPR RALPELVSPG RELGRVSAEA AGYTGLPVGL
     PVIAGASDKS CEVLGAGCLS PHQGCIGYGT TATINVNCDK YIEPIALVPP YPSAKAGSYN
     LEVQIFRGFW MVSWFKEQFA QLEQEAARLR GVEAEVLLEE LASDVPAGSM GLVLQPFWSP
     GLRHPGPEAK GAIIGFGGAH KKQHLYRAML EGLAFALRDG RERIQRRDKT KLSELYVCGG
     GSRSDLAMQI TADVFNLPAS RPAHFEASGL GAAMLACLGC GLHEDLSGAV RAMTATGRTF
     EPDRSNVGVY DELYDKVYRR MYKRLRPFYQ RIMAVTGYPA PAGKD
//
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