HIS4_SALTY
ID HIS4_SALTY Reviewed; 245 AA.
AC P10372;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
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=STM2076;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT "Structure and function of the Salmonella typhimurium and Escherichia coli
RT K-12 histidine operons.";
RL J. Mol. Biol. 203:585-606(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; X13464; CAA31827.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20980.1; -; Genomic_DNA.
DR PIR; JS0161; ISEBIC.
DR RefSeq; NP_461021.1; NC_003197.2.
DR RefSeq; WP_000586409.1; NC_003197.2.
DR PDB; 5A5W; X-ray; 1.60 A; A=1-245.
DR PDB; 5AB3; X-ray; 1.80 A; A/B/C=1-245.
DR PDB; 5ABT; X-ray; 1.65 A; A=1-245.
DR PDB; 5AC6; X-ray; 1.99 A; A=1-245.
DR PDB; 5AC7; X-ray; 1.90 A; A/B=1-245.
DR PDB; 5AC8; X-ray; 1.70 A; A=1-245.
DR PDB; 5AHE; X-ray; 1.70 A; A=1-245.
DR PDB; 5AHF; X-ray; 2.20 A; A=1-245.
DR PDB; 5AHI; X-ray; 2.00 A; A=1-245.
DR PDB; 5G1T; X-ray; 1.70 A; A=1-245.
DR PDB; 5G1Y; X-ray; 1.80 A; A=1-15, A=17-245.
DR PDB; 5G2H; X-ray; 1.90 A; A=1-245.
DR PDB; 5G2I; X-ray; 1.60 A; A=1-15, A=17-245.
DR PDB; 5G2W; X-ray; 2.10 A; A=1-245.
DR PDB; 5G4E; X-ray; 2.65 A; A/B=1-15, A/B=17-245.
DR PDB; 5G4W; X-ray; 2.30 A; A=1-245.
DR PDB; 5G5I; X-ray; 2.00 A; A=1-245.
DR PDB; 5L6U; X-ray; 1.60 A; A=1-15, A=17-245.
DR PDB; 5L9F; X-ray; 2.59 A; A/B=1-245.
DR PDBsum; 5A5W; -.
DR PDBsum; 5AB3; -.
DR PDBsum; 5ABT; -.
DR PDBsum; 5AC6; -.
DR PDBsum; 5AC7; -.
DR PDBsum; 5AC8; -.
DR PDBsum; 5AHE; -.
DR PDBsum; 5AHF; -.
DR PDBsum; 5AHI; -.
DR PDBsum; 5G1T; -.
DR PDBsum; 5G1Y; -.
DR PDBsum; 5G2H; -.
DR PDBsum; 5G2I; -.
DR PDBsum; 5G2W; -.
DR PDBsum; 5G4E; -.
DR PDBsum; 5G4W; -.
DR PDBsum; 5G5I; -.
DR PDBsum; 5L6U; -.
DR PDBsum; 5L9F; -.
DR AlphaFoldDB; P10372; -.
DR SMR; P10372; -.
DR STRING; 99287.STM2076; -.
DR PaxDb; P10372; -.
DR EnsemblBacteria; AAL20980; AAL20980; STM2076.
DR GeneID; 1253597; -.
DR KEGG; stm:STM2076; -.
DR PATRIC; fig|99287.12.peg.2198; -.
DR HOGENOM; CLU_048577_1_2_6; -.
DR OMA; EWLHLVD; -.
DR PhylomeDB; P10372; -.
DR BioCyc; SENT99287:STM2076-MON; -.
DR BRENDA; 5.3.1.16; 5542.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Isomerase; Reference proteome.
FT CHAIN 1..245
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000142049"
FT ACT_SITE 7
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 123..124
FT /note="AL -> GV (in Ref. 1; CAA31827)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="H -> Q (in Ref. 1; CAA31827)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="G -> A (in Ref. 1; CAA31827)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="I -> DV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="V -> M (in Ref. 1; CAA31827)"
FT /evidence="ECO:0000305"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5G2I"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5A5W"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:5A5W"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:5A5W"
FT TURN 213..217
FT /evidence="ECO:0007829|PDB:5A5W"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:5A5W"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:5A5W"
SQ SEQUENCE 245 AA; 26089 MW; 20CF123F43DCE925 CRC64;
MIIPALDLID GTVVRLHQGD YARQRDYGND PLPRLQDYAA QGAGVLHLVD LTGAKDPAKR
QIPLIKTLVA GVNVPVQVGG GVRTEEDVAA LLKAGVARVV IGSTAVKSPD VVKGWFERFG
AQALVLALDV RIDEHGTKQV AVSGWQENSG VSLEQLVETY LPVGLKHVLC TDISRDGTLA
GSNVSLYEEV CARYPQIAFQ SSGGIGDIDD IAALRGTGVR GVIVGRALLE GKFTVKEAIQ
CWQNV
