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Database: UniProt
Entry: U7D826_9BACT
LinkDB: U7D826_9BACT
Original site: U7D826_9BACT 
ID   U7D826_9BACT            Unreviewed;       251 AA.
AC   U7D826;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=5-proFAR isomerase {ECO:0000256|ARBA:ARBA00031376};
GN   ORFNames=CALK_0813 {ECO:0000313|EMBL:ERP32093.1};
OS   Chitinivibrio alkaliphilus ACht1.
OC   Bacteria; Fibrobacterota; Chitinivibrionia; Chitinivibrionales;
OC   Chitinivibrionaceae; Chitinivibrio.
OX   NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP32093.1, ECO:0000313|Proteomes:UP000017148};
RN   [1] {ECO:0000313|EMBL:ERP32093.1, ECO:0000313|Proteomes:UP000017148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACht1 {ECO:0000313|EMBL:ERP32093.1,
RC   ECO:0000313|Proteomes:UP000017148};
RX   PubMed=24112708;
RA   Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA   Muyzer G., Mardanov A.V., Ravin N.V.;
RT   "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a novel
RT   extremely haloalkaliphilic anaerobic chitinolytic bacterium from the
RT   candidate phylum Termite Group 3.";
RL   Environ. Microbiol. 0:0-0(2013).
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:ERP32093.1}.
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DR   EMBL; ASJR01000006; ERP32093.1; -; Genomic_DNA.
DR   RefSeq; WP_022636324.1; NZ_ASJR01000006.1.
DR   AlphaFoldDB; U7D826; -.
DR   STRING; 1313304.CALK_0813; -.
DR   PATRIC; fig|1313304.3.peg.780; -.
DR   eggNOG; COG0106; Bacteria.
DR   OrthoDB; 9807749at2; -.
DR   Proteomes; UP000017148; 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:ERP32093.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017148}.
SQ   SEQUENCE   251 AA;  27876 MW;  66CD8931BA5E0176 CRC64;
     MNFKPCIDLH QGKVKQIVGA TLRDSDNYAK TNFESPHSPE YYARLYQRDN LRGGHVIMLG
     PGNEEAARDA LQTWPGGLQI GGGIRHDNAQ TYLDWGASHV IMTSFIFHDG HLNTANLKKT
     VQAIGKERLV LDLSCMKIDA TYYIVTNRWQ NVTTLAITQE TLEYLSQYCD EFLIHAAHVE
     GKMAGPDYEL ISLLGNNSPI TTTYAGGVHT LEDLTHIRKK GKNRIDITIG SALDIFGGPL
     PYTDIVAATK E
//
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