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Database: UniProt
Entry: R9NC45_9FIRM
LinkDB: R9NC45_9FIRM
Original site: R9NC45_9FIRM 
ID   R9NC45_9FIRM            Unreviewed;       256 AA.
AC   R9NC45;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=5-proFAR isomerase {ECO:0000256|ARBA:ARBA00031376};
GN   ORFNames=C817_01602 {ECO:0000313|EMBL:EOS80546.1};
OS   Dorea sp. 5-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1235798 {ECO:0000313|EMBL:EOS80546.1, ECO:0000313|Proteomes:UP000014211};
RN   [1] {ECO:0000313|EMBL:EOS80546.1, ECO:0000313|Proteomes:UP000014211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-2 {ECO:0000313|EMBL:EOS80546.1,
RC   ECO:0000313|Proteomes:UP000014211};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Dorea bacterium 5-2.";
RL   Submitted (APR-2013) 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:EOS80546.1}.
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DR   EMBL; ASTD01000030; EOS80546.1; -; Genomic_DNA.
DR   RefSeq; WP_016218344.1; NZ_KE159748.1.
DR   AlphaFoldDB; R9NC45; -.
DR   STRING; 1235798.C817_01602; -.
DR   PATRIC; fig|1235798.3.peg.1710; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_065050_0_0_9; -.
DR   OrthoDB; 9807749at2; -.
DR   Proteomes; UP000014211; 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:EOS80546.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014211}.
SQ   SEQUENCE   256 AA;  28594 MW;  CD823E220CE1F452 CRC64;
     MRFRPCIDIH NGTVKQIIGG SLTDENDQAA ENYSAVQDAD HFAELYRRDG LSGGHVILLN
     PPSSEYYEKT KEQAMKALRA FPQGLQVGGG ITAENAQEYL QAGASHVIVT SYVFRDGAIY
     WENMEKLRRA VGAEHVVIDL SCRKRDGDYY IVTNRWQTFT EVKLTQEVLE EIAGYCSEFL
     VHGVDVEGRA SGIEEDLVRL LGRHEKNAVT YAGGIGSLED LERLRVLSDG RVDFTIGSAL
     DLFGGGIPYE EIRRFR
//
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