ID HIS4_PROM9 Reviewed; 255 AA. AC Q31B81; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000255|HAMAP-Rule:MF_01014}; DE EC=5.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01014}; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000255|HAMAP-Rule:MF_01014}; GN Name=hisA {ECO:0000255|HAMAP-Rule:MF_01014}; GN OrderedLocusNames=PMT9312_0804; OS Prochlorococcus marinus (strain MIT 9312). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=74546; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9312; RX PubMed=16556843; DOI=10.1126/science.1122050; RA Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K., RA Delong E.F., Chisholm S.W.; RT "Genomic islands and the ecology and evolution of Prochlorococcus."; RL Science 311:1768-1770(2006). CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D- CC ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5- CC phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469, CC ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01014}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC {ECO:0000255|HAMAP-Rule:MF_01014}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01014}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP- CC Rule:MF_01014}. 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; CP000111; ABB49864.1; -; Genomic_DNA. DR RefSeq; WP_011376359.1; NC_007577.1. DR AlphaFoldDB; Q31B81; -. DR SMR; Q31B81; -. DR STRING; 74546.PMT9312_0804; -. DR KEGG; pmi:PMT9312_0804; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_1_3; -. DR OrthoDB; 9807749at2; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000002715; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd04732; HisA; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01014; HisA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR006063; HisA_bact_arch. DR InterPro; IPR044524; Isoase_HisA-like. DR InterPro; IPR023016; Isoase_HisA-like_bact. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR00007; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; 1. DR PANTHER; PTHR43090; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1. DR PANTHER; PTHR43090:SF2; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase. FT CHAIN 1..255 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000229069" FT ACT_SITE 8 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" FT ACT_SITE 129 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" SQ SEQUENCE 255 AA; 28241 MW; 9419CD9D1B76C2A1 CRC64; MELIPAIDLM NGKCVRLFKG DFNKRKDFTK EPHEQAKYWE SEGAKYIHIV DLDAAKTGSP TNDKSIKDIA KTVNIPIQIG GGIRSQERIE QLFSYGIEKV IMGTSAIENK ELVKDLSNKF PGRIIVGIDA KDGKVSTRGW LEQSNILATD LVREFSSFKI ASFIVTDINT DGTLEGTNEE FIKRILEITD IPVIASGGVG SISDLLSLVK LENSGLFGVI VGKALYENKF KISEAINVLS SERLTDFDLN NNYYA //