HIS4_ACIBC
ID HIS4_ACIBC Reviewed; 243 AA.
AC B2I0N7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
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}; OrderedLocusNames=ACICU_03434;
OS Acinetobacter baumannii (strain ACICU).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=405416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACICU;
RX PubMed=18411315; DOI=10.1128/aac.01643-07;
RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT Acinetobacter baumannii strain belonging to the European clone II group.";
RL Antimicrob. Agents Chemother. 52:2616-2625(2008).
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}.
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DR EMBL; CP000863; ACC58743.1; -; Genomic_DNA.
DR RefSeq; WP_000905538.1; NZ_CP031380.1.
DR AlphaFoldDB; B2I0N7; -.
DR SMR; B2I0N7; -.
DR GeneID; 60752397; -.
DR GeneID; 66395577; -.
DR KEGG; abc:ACICU_03434; -.
DR HOGENOM; CLU_048577_1_1_6; -.
DR OMA; EWLHLVD; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000008839; 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; -; 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 PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00007; TIGR00007; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase.
FT CHAIN 1..243
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_1000135067"
FT ACT_SITE 8
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ SEQUENCE 243 AA; 26083 MW; 7EEE51B81AB372B7 CRC64;
MLIIPAIDLK DGKCVRLKQG RMEDDTVFSD DPVATAQHWV NEGARRLHLV DLNGAFAGTP
IHKPVVEAIA KAQPELPIQI GGGIRSLETI EHYLEAGVTF VIIGTKAVQE PEFVEEACKR
FAGHIIVGID AMNGMVATDG WANVTDVKAT DLAKRFADAG VSSIVYTDIA RDGMMQGVNV
EQTVNLAQYS GLPVIASGGV TNLDDVRNLK GQPGILGAIT GRAIYEGTLN LREAQLLLDE
NRL
