HIS4_COREF
ID HIS4_COREF Reviewed; 246 AA.
AC Q8FNZ7;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=CE1996;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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}.
CC -!- CAUTION: Ala-129 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; BA000035; BAC18806.1; -; Genomic_DNA.
DR RefSeq; WP_006767994.1; NZ_GG700683.1.
DR PDB; 4AXK; X-ray; 2.25 A; A/B=1-246.
DR PDBsum; 4AXK; -.
DR AlphaFoldDB; Q8FNZ7; -.
DR SMR; Q8FNZ7; -.
DR STRING; 196164.23493837; -.
DR EnsemblBacteria; BAC18806; BAC18806; BAC18806.
DR KEGG; cef:CE1996; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_11; -.
DR OMA; EWLHLVD; -.
DR OrthoDB; 794219at2; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000001409; 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:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:InterPro.
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; IPR010188; HisA/PriA_Actinobacteria.
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; TIGR01919; hisA-trpF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Isomerase; Reference proteome.
FT CHAIN 1..246
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000142000"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:4AXK"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:4AXK"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:4AXK"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:4AXK"
SQ SEQUENCE 246 AA; 26624 MW; EF62454178C09B50 CRC64;
MTFTILPAVD VVNGQAVRLD QGEAGTEKSY GTPLESALRW QEQGAEWLHF VDLDAAFNRG
SNHELMAEIT RQLDIKVELT GGIRDDASLE RALATGATRV NIGTAALEKP EWIADVIRRH
GEKIAVDIAV RLENGEWRTK GNGWVSDGGD LWEVLERLDS QGCSRFVVTD VSKDGTLTGP
NVDLLRDVAA ATDAPIVASG GISTLEDVLG LAKYQDEGID SVIIGKALYE HRFTLAEALE
AVEKLG
