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 27-MAR-2024, entry version 116.
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 ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC 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=ATCC 33912 / 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., Golden S., 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; NZ_JACJTX010000001.1.
DR AlphaFoldDB; Q8GJM0; -.
DR SMR; Q8GJM0; -.
DR STRING; 1140.Synpcc7942_1829; -.
DR PaxDb; 1140-Synpcc7942_1829; -.
DR GeneID; 76400557; -.
DR KEGG; syf:Synpcc7942_1829; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_3; -.
DR OrthoDB; 9807749at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1829-MONOMER; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000889800; 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_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
//
