ID A0A090X4L7_9FLAO Unreviewed; 490 AA. AC A0A090X4L7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 11-NOV-2015, entry version 10. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|RuleBase:RU003928}; DE EC=1.1.1.205 {ECO:0000256|RuleBase:RU003928}; GN ORFNames=JCM19274_4501 {ECO:0000313|EMBL:GAL78002.1}; OS Algibacter lectus. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Algibacter. OX NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL78002.1}; RN [1] {ECO:0000313|EMBL:GAL78002.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCM 19274 {ECO:0000313|EMBL:GAL78002.1}; RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K., RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., RA Niwa A., Sawabe T., Sawabe T.; RT "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus RT Strains SS8 and NR4."; RL Genome Announc. 2:e01168-14(2014). CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. {ECO:0000256|RuleBase:RU003928}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. {ECO:0000256|RuleBase:RU003928}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC {ECO:0000256|RuleBase:RU003927}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAL78002.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BBNU01000002; GAL78002.1; -; Genomic_DNA. DR RefSeq; WP_042495518.1; NZ_BBNU01000002.1. DR EnsemblBacteria; GAL78002; GAL78002; JCM19274_4501. DR UniPathway; UPA00601; UER00295. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 2. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 3: Inferred from homology; KW GMP biosynthesis {ECO:0000256|RuleBase:RU003928}; KW Metal-binding {ECO:0000256|RuleBase:RU003928}; KW NAD {ECO:0000256|RuleBase:RU003928}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003927, KW ECO:0000313|EMBL:GAL78002.1}; KW Potassium {ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|RuleBase:RU003928}. FT ACT_SITE 308 308 Thioimidate intermediate. FT {ECO:0000256|PIRSR:PIRSR000130-1}. SQ SEQUENCE 490 AA; 52108 MW; 6875B10DE404887F CRC64; MTAHENKIVG EGLTYDDVLL VPAFSEVLPR EVSIQTKFTR NITINVPIIS AAMDTVTESK MAIAMAQEGG IGVLHKNMSI EAQALKVRRV KRAESGMIID PVTLPVTAVV SDAKKYMAEY SIGGIPIVAE DGTLKGIVTN RDLRFEHNGK RAISEVMTSE KLVTASVGTS LKDAELILQE HKIEKLLIVD DNFKLSGLIT FRDITKLSQK PNANKDQYGR LRVAAALGVT ADAVERAEAL VNAGVDAVVI DTAHGHTKGV VSVLKTIKAK FPNLDVIVGN IATGAAAKYL VEAGADAVKV GIGPGSICTT RVVAGVGFPQ FSAVLEVAAA IKGSGVPVIA DGGIRYTGDI PKAIAAGADT VMLGSLLAGT KESPGETIIY EGRKFKSYRG MGSVEAMKEG SKDRYFQDVE DDIKKLVPEG IVGRVPYKGD LYESIHQFIG GLRAGMGYCG AKDIETLKET GQFVKITASG INESHPHDVT ITKESPNYSR //