ID K5WJ01_PHACS Unreviewed; 266 AA.
AC K5WJ01;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|ARBA:ARBA00018464, ECO:0000256|RuleBase:RU364022};
DE EC=5.3.1.16 {ECO:0000256|ARBA:ARBA00012550, ECO:0000256|RuleBase:RU364022};
DE AltName: Full=5-proFAR isomerase {ECO:0000256|ARBA:ARBA00031376, ECO:0000256|RuleBase:RU364022};
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000256|ARBA:ARBA00030547, ECO:0000256|RuleBase:RU364022};
GN ORFNames=PHACADRAFT_136930 {ECO:0000313|EMBL:EKM59335.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM59335.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM59335.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM59335.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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|RuleBase:RU364022};
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|RuleBase:RU364022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364022}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|RuleBase:RU003657}.
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DR EMBL; JH930469; EKM59335.1; -; Genomic_DNA.
DR RefSeq; XP_007391899.1; XM_007391837.1.
DR AlphaFoldDB; K5WJ01; -.
DR STRING; 650164.K5WJ01; -.
DR GeneID; 18908373; -.
DR KEGG; pco:PHACADRAFT_136930; -.
DR HOGENOM; CLU_065050_0_0_1; -.
DR InParanoid; K5WJ01; -.
DR OrthoDB; 312953at2759; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000008370; Unassembled WGS sequence.
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-EC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04723; HisA_HisF; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011858; His6-like_euk.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR044524; Isoase_HisA-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR02129; hisA_euk; 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|RuleBase:RU003657};
KW Cytoplasm {ECO:0000256|RuleBase:RU364022};
KW Histidine biosynthesis {ECO:0000256|RuleBase:RU003657};
KW Isomerase {ECO:0000256|RuleBase:RU364022};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370}.
SQ SEQUENCE 266 AA; 28772 MW; FDD04D3CDCB6F9BF CRC64;
MAGQQSRTLF KPCIDLHGGH VKQIVGGTLS DAPESLKTNF VATKPTAYYA ELYKEHGLEG
GHVIMLGKGN NDAAKEALAA WPGGLQVGGG ITDQNCQAWI GAGASKVIVT SFLFPEGKFS
LERLEKISSL VGKDSLVVDV SCRRKDSRWF VAMDKWQRIT EMEVCKESLD TLAKYCSEFL
IHAADVEGLC QGIDEDLVKK LGEWVTIPTT YAGGARSISD LDLVDNLSGG KVDLTYGSSL
DIFGGSLVNF DELVLYNTVA QKAMQQ
//
