ID   HIS4_IDILO              Reviewed;         245 AA.
AC   Q5QWQ6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
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}; OrderedLocusNames=IL1839;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017340; AAV82671.1; -; Genomic_DNA.
DR   RefSeq; WP_011235071.1; NC_006512.1.
DR   AlphaFoldDB; Q5QWQ6; -.
DR   SMR; Q5QWQ6; -.
DR   STRING; 283942.IL1839; -.
DR   PRIDE; Q5QWQ6; -.
DR   EnsemblBacteria; AAV82671; AAV82671; IL1839.
DR   KEGG; ilo:IL1839; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_048577_1_2_6; -.
DR   OMA; EWLHLVD; -.
DR   OrthoDB; 794219at2; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000001171; 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; -; 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;
KW   Reference proteome.
FT   CHAIN           1..245
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_0000229060"
FT   ACT_SITE        7
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"
SQ   SEQUENCE   245 AA;  26710 MW;  D27121D0ED15B19D CRC64;
     MLIPALDLID GKVVRLYQGD FAQKTEFDLT PLGQAQLYAQ AGAEWLHLVD LDGAKDPDKR
     QQKLLAKLAS DSGMKCQAGG GIRTTEDLEA LFDAGIERAV IGSTAVNQPD TVKQWFQAYG
     GEKIVLALDV NIDQSGNAMV ATHGWQQAST HTLDDILNRY LDLGCRHVLC TDISKDGTMT
     GTNVELYKRY KQLYPQVVWQ ASGGVSCLDD LKDLKAVNCD SVILGKSLLT GAFTMQEALA
     CWQNA