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Database: UniProt
Entry: J7L0W5_NOCAA
LinkDB: J7L0W5_NOCAA
Original site: J7L0W5_NOCAA 
ID   J7L0W5_NOCAA            Unreviewed;       252 AA.
AC   J7L0W5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   OrderedLocusNames=B005_3838 {ECO:0000313|EMBL:AFR06421.1};
OS   Nocardiopsis alba (strain ATCC BAA-2165 / BE74).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR06421.1, ECO:0000313|Proteomes:UP000003779};
RN   [1] {ECO:0000313|EMBL:AFR06421.1, ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RX   PubMed=23105086; DOI=10.1128/JB.01522-12;
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-Genome Sequence of Nocardiopsis alba Strain ATCC BAA-2165,
RT   Associated with Honeybees.";
RL   J. Bacteriol. 194:6358-6359(2012).
RN   [2] {ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 associated
RT   with honeybees.";
RL   Submitted (AUG-2012) 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|ARBA:ARBA00004496,
CC       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}.
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DR   EMBL; CP003788; AFR06421.1; -; Genomic_DNA.
DR   RefSeq; WP_014908888.1; NC_018524.1.
DR   AlphaFoldDB; J7L0W5; -.
DR   STRING; 1205910.B005_3838; -.
DR   KEGG; nal:B005_3838; -.
DR   PATRIC; fig|1205910.3.peg.3634; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_048577_1_1_11; -.
DR   OrthoDB; 9807749at2; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000003779; 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; 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:UP000003779}.
FT   ACT_SITE        19
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   252 AA;  26486 MW;  9B6BFDF7F3614C84 CRC64;
     MTGEHTPSTP ALELLPAVDV AGGQAVQLVQ GKAGTGGRYG DPFKAAEAWQ NAGAEWVHLV
     DLDAAFGRGE NRELLREIVG RLDIKVEMSG GIRDDESLKA ALDTGCARVN IGTAALENPE
     WCARIIADHG DRIAIGLDVR GTTLAARGWT RDGGDLFQTL ERLEAEGCAR YVVTDVNKDG
     TLKGPNLDLL RTVCEHTDKP VVASGGVSSL ADLEALSTLV PVGVEGAIMG TALYEGAFTL
     EDALALVKGG RR
//
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