ID K2H0A6_9BACT Unreviewed; 480 AA.
AC K2H0A6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=GMP reductase {ECO:0000256|ARBA:ARBA00015800};
DE EC=1.7.1.7 {ECO:0000256|ARBA:ARBA00012678};
GN ORFNames=ACD_2C00209G0004 {ECO:0000313|EMBL:EKE29190.1};
OS uncultured bacterium (gcode 4).
OC Bacteria; environmental samples.
OX NCBI_TaxID=1234023 {ECO:0000313|EMBL:EKE29190.1};
RN [1] {ECO:0000313|EMBL:EKE29190.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKE29190.1}.
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DR EMBL; AMFJ01000209; EKE29190.1; -; Genomic_DNA.
DR AlphaFoldDB; K2H0A6; -.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd02205; CBS_pair_SF; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS51371; CBS; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; NAD {ECO:0000256|PIRSR:PIRSR000130-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Potassium {ECO:0000256|PIRSR:PIRSR000130-4}.
FT DOMAIN 94..154
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 246..248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 304
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
SQ SEQUENCE 480 AA; 57961 MW; 51EC5709991A2FB3 CRC64;
MRFNNPNYEN EELAYEDVFL FQNYFEWTSR FWGIDIRPAF SFWTSIPIVS ANMNAVTGKR
MCEALARLWG LWILPQDMDI ETMCRIVTEI KWASIKFDTP VTVKSHHTIR DALWIIYKRS
HNAVIMTDDD NRPTGIFTLK DFNDLDQYTQ LWSLKKSFLI TWTEDITDEE AFDLMEDKWI
SSLPIVCENW KLLWILTKKQ TVRNSIYKPT LDNNWRLDLW VALWINQFME KARTLIKMWV
SIFVLDTAHG YQKKMLDAIM QFRSEFWDDP ILIAWNVITE EWTRTLIEAW ANWVKVWVWP
WAMCTTRMKT WVWRPQFTAV RKCSLEAKRL GWFIWADGGI KEPRDLVLAL AAWANHVMIW
TLFSWTYEST GDIKFDETWR MYKANYWMAS RKAVTLRNSG ISNFELARKA LFKEGISASK
IFIKEWREWV GDIVDEFMTW LRSSMTYIWW ENLEKFNEKS IIWVQTNAWF YEWTPHWKVR
//
