ID   HIS4_SHEB9              Reviewed;         245 AA.
AC   A9L4B9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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};
GN   OrderedLocusNames=Sbal195_2541;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000891; ABX49709.1; -; Genomic_DNA.
DR   RefSeq; WP_006086290.1; NC_009997.1.
DR   AlphaFoldDB; A9L4B9; -.
DR   SMR; A9L4B9; -.
DR   EnsemblBacteria; ABX49709; ABX49709; Sbal195_2541.
DR   GeneID; 11772643; -.
DR   KEGG; sbn:Sbal195_2541; -.
DR   HOGENOM; CLU_048577_1_2_6; -.
DR   OMA; EWLHLVD; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000000770; 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.
FT   CHAIN           1..245
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_1000084112"
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;  26073 MW;  039F303FE7A7758D CRC64;
     MIIPAIDLID GNVVRLYQGD YGQQTTFDLS PLAQLQSYEA QGAKWLHIVD LTGAKDPAKR
     QTRLISQIVA GLNANIQVGG GIRTEEQVTE LLNIGVKRVV IGSLAVKEPE LVKQWFIKYG
     SEAICLALDV NINQSGEKIV AVSGWQSGGG KSLESLVETF SAVGLKHALV TDISRDGTLT
     GANTALYQEI AASYPDIAWQ ASGGIATLDD VAAVRDSGAA GIIIGKALLI NQFNVVEAIQ
     CWPND