ID D2RYU4_HALTV Unreviewed; 374 AA.
AC D2RYU4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=GMP reductase {ECO:0000313|EMBL:ADB61912.1};
DE EC=1.7.1.7 {ECO:0000313|EMBL:ADB61912.1};
GN OrderedLocusNames=Htur_3045 {ECO:0000313|EMBL:ADB61912.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB61912.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB61912.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC {ECO:0000256|ARBA:ARBA00005502}.
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DR EMBL; CP001860; ADB61912.1; -; Genomic_DNA.
DR RefSeq; WP_012944175.1; NC_013743.1.
DR AlphaFoldDB; D2RYU4; -.
DR STRING; 543526.Htur_3045; -.
DR GeneID; 8743664; -.
DR KEGG; htu:Htur_3045; -.
DR eggNOG; arCOG00612; Archaea.
DR HOGENOM; CLU_022552_5_3_2; -.
DR OrthoDB; 324877at2157; -.
DR Proteomes; UP000001903; Chromosome.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR Pfam; PF00478; IMPDH; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:ADB61912.1}.
FT DOMAIN 7..336
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT REGION 334..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 38413 MW; 83D060189339C729 CRC64;
MNDLRTGLSY GDVLLVPNRS PVDSRSDVDL STRLTPSVEL ETPLVSAAMD TVTEAELAIA
LSRAGGFGVL HRFLTPAEQA EQVARVKNAD EQVGAAIGID EDFVGRGGAL VEAGVDALVV
DVAHGHMERT IDAVARLREE FPETDLVAGN VATPAGVEDL AAAGADCVKV GIGPGSHCTT
RKVAGAGVPQ LTAVDDCAEA AEALDVTICA DGGIRTSGDA VKALMAGADT VMMGSLFAGT
EEAPGAVVEV DGTRYKRSRG MATTTAAEKR DDKEEDVRAD EGVEALTPYK GPVADVVAEF
CAGIQSGLSY CGGHTIPEAR EKAEFIRVAA SAKEREGYHA DHDWEGVDVD STAKAGGGSG
SEDGSANATA EGDD
//
