ID HIS4_XYLFA Reviewed; 265 AA. AC Q9PBC9; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; DE EC=5.3.1.16; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; GN Name=hisA; OrderedLocusNames=XF_2215; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=160492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). 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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. 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; AE003849; AAF85014.1; -; Genomic_DNA. DR PIR; B82585; B82585. DR RefSeq; WP_010894663.1; NC_002488.3. DR AlphaFoldDB; Q9PBC9; -. DR SMR; Q9PBC9; -. DR STRING; 160492.XF_2215; -. DR KEGG; xfa:XF_2215; -. DR PATRIC; fig|160492.11.peg.2357; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_2_6; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000812; 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..265 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000142078" FT ACT_SITE 10 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 132 FT /note="Proton donor" FT /evidence="ECO:0000250" SQ SEQUENCE 265 AA; 28229 MW; 2563784C190A516B CRC64; MNFIVYPALD IRNGAVVRLQ QGDYARQTRY DDQVLPRALA FADSGATWMH LVDLDAAKAG GYTLAPLLRQ MTRATGLQVQ TGGGVRSRDD VARILDAGAA RVVIGSLAVR ESARVIEWLQ AFGPERITVA LDTRQDAGGV WRLPVHGWTE VAEATLDVLA QQYAAAGLRH LLCTDIARDG MLSGPNMDVY TYLRALVPAV QLQVSGGARD VADVVAAKMA GCAGIVLGKA LLEGRLALKE AVQQGSVADP SDPLPCGELT EPVCR //