ID   HIS4_PICP2              Reviewed;         256 AA.
AC   B1XQI2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
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};
GN   OrderedLocusNames=SYNPCC7002_A1890;
OS   Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Picosynechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) 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: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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000951; ACA99877.1; -; Genomic_DNA.
DR   RefSeq; WP_012307500.1; NZ_JAHHPU010000002.1.
DR   AlphaFoldDB; B1XQI2; -.
DR   SMR; B1XQI2; -.
DR   STRING; 32049.SYNPCC7002_A1890; -.
DR   KEGG; syp:SYNPCC7002_A1890; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_048577_1_1_3; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000001688; 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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR006063; HisA_bact_arch.
DR   InterPro; IPR044524; Isoase_HisA-like.
DR   InterPro; IPR023016; Isoase_HisA-like_bact.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00007; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; 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; Cytoplasm; Histidine biosynthesis; Isomerase;
KW   Reference proteome.
FT   CHAIN           1..256
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_1000190564"
FT   ACT_SITE        8
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   256 AA;  26489 MW;  CD6B3EF50DA62BCA CRC64;
     MEVIPAIDLL GGQCVRLYQG DYQQAQVFNN DPVQVARTWA EQGATRLHVV DLDGAKQGES
     VNLGAIAKIA AAIDIPVQVG GGLRTVESVA QLFDVGVERA ILGTAAVDNP DLVTELCAKY
     PGRIAVGIDA RDGKVATKGW LETSAVLATD LAKQMATQGV AAIIYTDIHR DGTMAGPNLE
     ALRELAATIE IPVIASGGVS SLADLVNLVA LEGIGVTGAI VGRAIYTGDI NLAEAVKAVG
     PQRLQDVFPD DGTAIA
//