ID A0A1H5WQI0_9EURY Unreviewed; 241 AA.
AC A0A1H5WQI0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|ARBA:ARBA00018464, ECO:0000256|HAMAP-Rule:MF_01014};
DE EC=5.3.1.16 {ECO:0000256|ARBA:ARBA00012550, 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=DV707_01005 {ECO:0000313|EMBL:QCC46368.1}, SAMN04488133_1359
GN {ECO:0000313|EMBL:SEG01611.1};
OS Halobellus limi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=699433 {ECO:0000313|EMBL:SEG01611.1, ECO:0000313|Proteomes:UP000236740};
RN [1] {ECO:0000313|EMBL:SEG01611.1, ECO:0000313|Proteomes:UP000236740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:SEG01611.1,
RC ECO:0000313|Proteomes:UP000236740};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCC46368.1, ECO:0000313|Proteomes:UP000296733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:QCC46368.1,
RC ECO:0000313|Proteomes:UP000296733};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
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, ECO:0000256|RuleBase:RU003658};
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 ECO:0000256|RuleBase:RU003658}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014,
CC ECO:0000256|RuleBase:RU003658}.
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; CP031311; QCC46368.1; -; Genomic_DNA.
DR EMBL; FNVN01000001; SEG01611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5WQI0; -.
DR KEGG; hlm:DV707_01005; -.
DR OrthoDB; 52866at2157; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000236740; Unassembled WGS sequence.
DR Proteomes; UP000296733; 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:SF7; 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|HAMAP-Rule:MF_01014,
KW ECO:0000256|RuleBase:RU003657};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01014,
KW ECO:0000256|RuleBase:RU003657};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01014};
KW Reference proteome {ECO:0000313|Proteomes:UP000236740}.
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ SEQUENCE 241 AA; 25038 MW; 4E1E08263C625AC1 CRC64;
MSDPFPDFEV VPAVDMQDGE VVQLVQGERG TEKRYGDPVA AAERWVDAGA ETLHLVDLDG
AFEGERGNAD AVEAVVEAVD VPVQLGGGIR TADDATDLLD RGVERVILGT AAVENPDLVA
EISEGYPGRV MVSLDARDGE VVVSGWTEGT GLDPAEAASR YEELGAGSIL FTDVDVEGKQ
EGVQTEVTRR VVEAVDVPVV ASGGVASLDD VRALRDAGAA AVVVGTALYE GAFTLAAAMR
V
//