HIS4_RHOBA
ID HIS4_RHOBA Reviewed; 253 AA.
AC Q7UG70;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=RB8080;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294147; CAD78459.1; -; Genomic_DNA.
DR RefSeq; NP_868181.1; NC_005027.1.
DR AlphaFoldDB; Q7UG70; -.
DR SMR; Q7UG70; -.
DR STRING; 243090.RB8080; -.
DR EnsemblBacteria; CAD78459; CAD78459; RB8080.
DR KEGG; rba:RB8080; -.
DR PATRIC; fig|243090.15.peg.3904; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_0; -.
DR InParanoid; Q7UG70; -.
DR OMA; EWLHLVD; -.
DR OrthoDB; 794219at2; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..253
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000142045"
FT ACT_SITE 19
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ SEQUENCE 253 AA; 27502 MW; 5B09803229D1803B CRC64;
MSSQTPGSEP RMEIWPAIDL RHGKPVRLRQ GDYDQQTTFG DDPVEFAKRW QESGAKRLHL
VDLDAARGDS PDANRDAVQR IIEATGLPCQ MGGGVRDEIT IESLLNVGVT RLVVGSRALK
DPDWFVEMCD KYPGKLVAGI DARDGKVATQ GWLETSDVSA FEFATKLRSR TENIAAIVYT
DIAKDGMMQG PNFEGLAEMA AASDIPLVAS GGVTTYDDIK QLVEMKMPAA IVGRSLYDGV
MELGEVVRLA GDV
