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Database: UniProt
Entry: A0A0D0IVU3_9MICO
LinkDB: A0A0D0IVU3_9MICO
Original site: A0A0D0IVU3_9MICO 
ID   A0A0D0IVU3_9MICO        Unreviewed;       249 AA.
AC   A0A0D0IVU3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|HAMAP-Rule:MF_01014};
DE            EC=5.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01014};
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000256|HAMAP-Rule:MF_01014};
GN   Name=hisA {ECO:0000256|HAMAP-Rule:MF_01014};
GN   ORFNames=SD72_00375 {ECO:0000313|EMBL:KIP53713.1};
OS   Leucobacter komagatae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=55969 {ECO:0000313|EMBL:KIP53713.1, ECO:0000313|Proteomes:UP000032120};
RN   [1] {ECO:0000313|EMBL:KIP53713.1, ECO:0000313|Proteomes:UP000032120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM ST2845 {ECO:0000313|EMBL:KIP53713.1,
RC   ECO:0000313|Proteomes:UP000032120};
RA   Karlyshev A.V., Kudryashova E.B.;
RT   "Draft genome sequence of Leucobacter komagatae strain VKM ST2845.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000901, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00005133, ECO:0000256|HAMAP-Rule:MF_01014}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01014,
CC       ECO:0000256|RuleBase:RU003657}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIP53713.1}.
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DR   EMBL; JXSQ01000001; KIP53713.1; -; Genomic_DNA.
DR   RefSeq; WP_042542452.1; NZ_JXSQ01000001.1.
DR   AlphaFoldDB; A0A0D0IVU3; -.
DR   OrthoDB; 9807749at2; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000032120; Unassembled WGS sequence.
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; Aldolase class I; 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   NCBIfam; TIGR01919; hisA-trpF; 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01014}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01014};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032120}.
FT   ACT_SITE        17
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT   ACT_SITE        138
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   249 AA;  26299 MW;  76A38E51E92A43FB CRC64;
     MTELATSPKL QLLPAIDMVD GKAVRLTQGA AGTETNYGSP VDAAMDWIEQ GAEWIHLVDL
     DAAFGRGSNV GIARKIIARA GNRVKIEFSG GIRDDKSLEA ALEMGAARVN LGTAALENPE
     WTRAVIAHYG EQIAVGLDVR GETLAARGWT EEGGNLWDVL ERLEEAGCPR YVVTDVTKDG
     MMAGPNVELL TKVCSRTNRP VIASGGISSL DDIAALREVV SRGVEGAIIG KALYDGAFTL
     PAALDVAGR
//
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