ID   HIS4_METVA              Reviewed;         238 AA.
AC   P05324;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   13-SEP-2023, entry version 105.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase;
DE            EC=5.3.1.16;
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
GN   Name=hisA;
OS   Methanococcus vannielii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3923489; DOI=10.1073/pnas.82.12.4207;
RA   Cue D., Beckler G.S., Reeve J.N., Konisky J.;
RT   "Structure and sequence divergence of two archaebacterial genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:4207-4211(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RX   PubMed=2829115; DOI=10.1093/nar/16.1.135;
RA   Brown J.W., Thomm M., Beckler G.S., Frey G., Stetter K.O., Reeve J.N.;
RT   "An archaebacterial RNA polymerase binding site and transcription
RT   initiation of the hisA gene in Methanococcus vannielii.";
RL   Nucleic Acids Res. 16:135-150(1988).
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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; M11219; AAA72490.1; -; Genomic_DNA.
DR   EMBL; X07391; CAA30300.1; -; Genomic_DNA.
DR   PIR; S00580; S00580.
DR   PIR; T48888; T48888.
DR   AlphaFoldDB; P05324; -.
DR   SMR; P05324; -.
DR   UniPathway; UPA00031; UER00009.
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; Cytoplasm; Histidine biosynthesis; Isomerase.
FT   CHAIN           1..238
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_0000142098"
FT   ACT_SITE        8
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        26
FT                   /note="H -> Q (in Ref. 2; CAA30300)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   238 AA;  25712 MW;  5082D2AF54D9E756 CRC64;
     MLIIPAVDMK NKKCVQLIQG NPDKKHVELD NPPEIAKKWV EQGAEMLHLV NLDGAINGKR
     VNDEFIEETI KNSGVPVQIG GGIRSVSDAL YFIEKGAEKV ILGTVAIQNP KIVREISSIV
     GKEKVTVALD AKDGKVLIKG WTEKTDYSPV QIGKILENMG AGSILFTNVD SEGLLEGINV
     LPTKELVDNL NIPIIASGGV TTVEDLLKFK EIGVYAVVVG SALYKDMINL KDAILASK
//