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HIS4_SYNE7
ID   HIS4_SYNE7              Reviewed;         256 AA.
AC   Q8GJM0; Q31M60;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 107.
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=Synpcc7942_1829; ORFNames=sen0020;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Holtman C.K., Sandoval P., Chen Y., Socias T., McMurtry S., Gonzalez A.,
RA   Salinas I., Golden S.S., Youderian P.;
RT   "Synechococcus elongatus PCC7942 cosmid 4G8.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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}.
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DR   EMBL; AY157498; AAN46174.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57859.1; -; Genomic_DNA.
DR   RefSeq; WP_011244575.1; NC_007604.1.
DR   AlphaFoldDB; Q8GJM0; -.
DR   SMR; Q8GJM0; -.
DR   STRING; 1140.Synpcc7942_1829; -.
DR   PRIDE; Q8GJM0; -.
DR   EnsemblBacteria; ABB57859; ABB57859; Synpcc7942_1829.
DR   KEGG; syf:Synpcc7942_1829; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_048577_1_1_3; -.
DR   OMA; EWLHLVD; -.
DR   OrthoDB; 794219at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1829-MON; -.
DR   UniPathway; UPA00031; UER00009.
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; -; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase.
FT   CHAIN           1..256
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_0000142064"
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"
FT   CONFLICT        138..145
FT                   /note="RGWLEDSG -> GAAGRFW (in Ref. 1; AAN46174)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152..175
FT                   /note="AQQMADLGACALICTDIGRDGTLQ -> HSRWQTWRLRTDLHRHWARWHAS
FT                   (in Ref. 1; AAN46174)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="L -> F (in Ref. 1; AAN46174)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   256 AA;  26326 MW;  368F941D8BA49AA7 CRC64;
     MDVIPAIDLL GGQCVRLFQG DYDQAEVYGK DPVGMALRWA EAGAQRLHLV DLDGAKEGSP
     VNAEAIATIA QRLSIPVQVG GGLRDRDTVA RLLDSGVERA ILGTVAVERP ALVEALAGEF
     PGQIAVGIDA RSGKVATRGW LEDSGLTAVA LAQQMADLGA CALICTDIGR DGTLQGPNLE
     ELRAIAAAVS IPVIASGGVG SLTDLLSLLP LEAQGVSGVI VGKALYTGAV DLQEALRAIG
     SGRWQDVAVD DSSRLA
 
 
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