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Database: UniProt
Entry: A0A0M2PG90_9BACI
LinkDB: A0A0M2PG90_9BACI
Original site: A0A0M2PG90_9BACI 
ID   A0A0M2PG90_9BACI        Unreviewed;       254 AA.
AC   A0A0M2PG90;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=5-proFAR isomerase {ECO:0000256|ARBA:ARBA00031376};
GN   ORFNames=WQ54_12695 {ECO:0000313|EMBL:KKI91860.1};
OS   Bacillus sp. SA1-12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI91860.1, ECO:0000313|Proteomes:UP000034887};
RN   [1] {ECO:0000313|EMBL:KKI91860.1, ECO:0000313|Proteomes:UP000034887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1-12 {ECO:0000313|EMBL:KKI91860.1,
RC   ECO:0000313|Proteomes:UP000034887};
RA   Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT   nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|ARBA:ARBA00009667, 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:KKI91860.1}.
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DR   EMBL; LATZ01000019; KKI91860.1; -; Genomic_DNA.
DR   RefSeq; WP_046517162.1; NZ_LATZ01000019.1.
DR   AlphaFoldDB; A0A0M2PG90; -.
DR   PATRIC; fig|1455638.3.peg.2830; -.
DR   OrthoDB; 9807749at2; -.
DR   Proteomes; UP000034887; Unassembled WGS sequence.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
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|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003657};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW   ECO:0000256|RuleBase:RU003657}; Isomerase {ECO:0000313|EMBL:KKI91860.1}.
SQ   SEQUENCE   254 AA;  28560 MW;  5996B1D02B1D67F1 CRC64;
     MKFRPCIDIH QGKVKQIVGD TLGLVNQFVI ENFVSDYDSA YYASLFRNDN LNGGHVIMLG
     EGNKESALQA LKEFPLGLQI GGGITAENAS FYLENNASHV IVTSYIFNNG DINIDRLNKL
     VNEVGKEKLV IDLSCKQKNG KWFVVTNKWT TFSNFEINKS TIREIEKYCD ELLIHAVDVE
     GKRTGIEEDL VKKLTEWVTI PTTYAGGVRS IKDLENFLKV SNGKLDITIG SSLDLFGGDL
     SYSEVVRFYK NIHY
//
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