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Database: UniProt
Entry: A0A0F5N136_9MYCO
LinkDB: A0A0F5N136_9MYCO
Original site: A0A0F5N136_9MYCO 
ID   A0A0F5N136_9MYCO        Unreviewed;       261 AA.
AC   A0A0F5N136;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE            EC=4.3.2.10 {ECO:0000256|HAMAP-Rule:MF_01013};
DE   AltName: Full=IGP synthase cyclase subunit {ECO:0000256|HAMAP-Rule:MF_01013};
DE   AltName: Full=IGP synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE   AltName: Full=ImGP synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE            Short=IGPS subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
GN   Name=hisF {ECO:0000256|HAMAP-Rule:MF_01013,
GN   ECO:0000313|EMBL:TXI48005.1};
GN   ORFNames=E6Q54_24340 {ECO:0000313|EMBL:TXI48005.1}, WR43_03765
GN   {ECO:0000313|EMBL:KKC00754.1};
OS   Mycolicibacter arupensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=342002 {ECO:0000313|EMBL:KKC00754.1, ECO:0000313|Proteomes:UP000034416};
RN   [1] {ECO:0000313|Proteomes:UP000034416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUC1 {ECO:0000313|Proteomes:UP000034416};
RA   Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium arupense GUC1.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKC00754.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUC1 {ECO:0000313|EMBL:KKC00754.1};
RA   Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium arupense strain GUC1.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:TXI48005.1, ECO:0000313|Proteomes:UP000321797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin_29_2 {ECO:0000313|EMBL:TXI48005.1};
RA   Stamps B.W., Spear J.R.;
RT   "Metagenome Assembled Genomes from an Advanced Water Purification
RT   Facility.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC       AICAR and glutamate. The HisF subunit catalyzes the cyclization
CC       activity that produces IGP and AICAR from PRFAR using the ammonia
CC       provided by the HisH subunit. {ECO:0000256|ARBA:ARBA00025475,
CC       ECO:0000256|HAMAP-Rule:MF_01013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-
CC         phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-
CC         amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-
CC         erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate;
CC         Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475,
CC         ChEBI:CHEBI:58525; EC=4.3.2.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00000619, ECO:0000256|HAMAP-
CC         Rule:MF_01013};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC       {ECO:0000256|ARBA:ARBA00005091, ECO:0000256|HAMAP-Rule:MF_01013}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152,
CC       ECO:0000256|HAMAP-Rule:MF_01013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01013,
CC       ECO:0000256|RuleBase:RU003657}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKC00754.1}.
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DR   EMBL; LASW01000008; KKC00754.1; -; Genomic_DNA.
DR   EMBL; SSGD01000187; TXI48005.1; -; Genomic_DNA.
DR   RefSeq; WP_046188281.1; NZ_SSGD01000187.1.
DR   AlphaFoldDB; A0A0F5N136; -.
DR   STRING; 342002.BST15_04260; -.
DR   PATRIC; fig|342002.3.peg.1425; -.
DR   OrthoDB; 9781903at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000034416; Unassembled WGS sequence.
DR   Proteomes; UP000321797; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01013; HisF; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR004651; HisF.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00735; hisF; 1.
DR   PANTHER; PTHR21235:SF2; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF; 1.
DR   PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01013}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01013};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01013}.
FT   ACT_SITE        16
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ   SEQUENCE   261 AA;  26567 MW;  589A67F4014185F7 CRC64;
     MHKHSDVAVR VIPCLDVDGG RVVKGVNFAN LRDAGDPVEL AAAYDAEGAD ELTFLDVTAS
     SSGRATMLEV VARTADQVFI PLTVGGGVRT VADVDVLLRA GADKVSVNTA AIARPELLGE
     LSRQFGSQCI VLSVDARTVP AGSAPTASGW EVTTHGGRQG TGIDAVEWAV RGVELGVGEI
     LLNSMDADGT KAGFDLAMLR AVRAAVSVPV IASGGAGAAE HFAPAVAAGA DAVLAASVFH
     FRELTIGQVK AAMSAEGIVV R
//
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