ID A0A1R1MHS5_9GAMM Unreviewed; 480 AA.
AC A0A1R1MHS5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=GMP reductase {ECO:0000256|ARBA:ARBA00015800};
DE EC=1.7.1.7 {ECO:0000256|ARBA:ARBA00012678};
GN ORFNames=BGP75_03915 {ECO:0000313|EMBL:OMH39250.1};
OS Motiliproteus sp. MSK22-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Motiliproteus.
OX NCBI_TaxID=1897630 {ECO:0000313|EMBL:OMH39250.1, ECO:0000313|Proteomes:UP000187359};
RN [1] {ECO:0000313|EMBL:OMH39250.1, ECO:0000313|Proteomes:UP000187359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSK22-1 {ECO:0000313|EMBL:OMH39250.1,
RC ECO:0000313|Proteomes:UP000187359};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Motiliproteus sp. strain MSK22-1.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:OMH39250.1}.
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DR EMBL; MIEQ01000021; OMH39250.1; -; Genomic_DNA.
DR RefSeq; WP_076714884.1; NZ_MIEQ01000021.1.
DR AlphaFoldDB; A0A1R1MHS5; -.
DR STRING; 1897630.BGP75_03915; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000187359; Unassembled WGS sequence.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd02205; CBS_pair_SF; 1.
DR CDD; cd00381; IMPDH; 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; IPR005991; GUAB1.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR NCBIfam; TIGR01303; IMP_DH_rel_1; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS51371; CBS; 2.
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};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726};
KW Reference proteome {ECO:0000313|Proteomes:UP000187359}.
FT DOMAIN 95..154
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 155..213
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 247..249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 300
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"
FT BINDING 302
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"
FT BINDING 305
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; 51567 MW; 383DEF355276AF6D CRC64;
MRFLHPSFDE QLELSLDDVF LVPGYSNAGS RSMVDLTPRD FPGGSLPIVS ANMNAVTGKR
MAETMARYGG LGVLPQDMEI STVERIVSHI KQADVRYDTP LVVTAEAPLR DVRSIIRKRA
QDMVIVVDHE NRPLGIITHA DLPEHDLYTP AGQLMSQQMV TINIDTSNRS AFERMEEERV
ESAPVVDHQG CLVGVLSRDD AVRLEVLKPA LDAKARLMVG AAVAISAEVA ERIEQLVAIG
VDFVVLDTAH GHQQQMIDAI IAARQVAGKV LPIVAGNVCT AEGTKALLDA GADVVKVNVG
PGSMCTTRMQ TGVGRPTFSA VYNSVKEARR HGKHIWADGG VHFPRDVALY LAAGASRVMV
GTLLAGTYES PGDIKEDRDG KLYKENYGMA SSRAVHNRTA ALDAFDRAQK GLFQEGISSS
KVYLREGLSS VGDHLINIAT GVQSAFTYVG ATDTESFAKK AVIGVQTSAG FGEGKAQGKM
//
