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Database: UniProt
Entry: R5UBY5_9BACT
LinkDB: R5UBY5_9BACT
Original site: R5UBY5_9BACT 
ID   R5UBY5_9BACT            Unreviewed;       565 AA.
AC   R5UBY5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Formimidoyltransferase-cyclodeaminase {ECO:0000256|ARBA:ARBA00017787};
DE            EC=2.1.2.5 {ECO:0000256|ARBA:ARBA00012252};
DE            EC=4.3.1.4 {ECO:0000256|ARBA:ARBA00012998};
DE   AltName: Full=Formiminotransferase-cyclodeaminase {ECO:0000256|ARBA:ARBA00030029};
GN   ORFNames=BN754_01371 {ECO:0000313|EMBL:CCZ75778.1};
OS   Alistipes finegoldii CAG:68.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1263035 {ECO:0000313|EMBL:CCZ75778.1, ECO:0000313|Proteomes:UP000018154};
RN   [1] {ECO:0000313|EMBL:CCZ75778.1, ECO:0000313|Proteomes:UP000018154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:68 {ECO:0000313|Proteomes:UP000018154};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Folate-dependent enzyme, that displays both transferase and
CC       deaminase activity. Serves to channel one-carbon units from
CC       formiminoglutamate to the folate pool. {ECO:0000256|ARBA:ARBA00025506}.
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005082}.
CC   -!- SUBUNIT: Homooctamer, including four polyglutamate binding sites. The
CC       subunits are arranged as a tetramer of dimers, and form a planar ring-
CC       shaped structure. {ECO:0000256|ARBA:ARBA00025915}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Golgi
CC       apparatus {ECO:0000256|ARBA:ARBA00004555}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       cyclodeaminase/cyclohydrolase family. {ECO:0000256|ARBA:ARBA00010825}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       formiminotransferase family. {ECO:0000256|ARBA:ARBA00008297}.
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:CCZ75778.1}.
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DR   EMBL; CBAO010000073; CCZ75778.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5UBY5; -.
DR   UniPathway; UPA00379; UER00555.
DR   Proteomes; UP000018154; Unassembled WGS sequence.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0030412; F:formimidoyltetrahydrofolate cyclodeaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030409; F:glutamate formimidoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.120.680; Formiminotetrahydrofolate cyclodeaminase monomer, up-and-down helical bundle; 1.
DR   Gene3D; 3.30.70.670; Formiminotransferase, C-terminal subdomain; 1.
DR   Gene3D; 3.30.990.10; Formiminotransferase, N-terminal subdomain; 1.
DR   InterPro; IPR007044; Cyclodeamin/CycHdrlase.
DR   InterPro; IPR013802; Formiminotransferase_C.
DR   InterPro; IPR037070; Formiminotransferase_C_sf.
DR   InterPro; IPR004227; Formiminotransferase_cat.
DR   InterPro; IPR012886; Formiminotransferase_N.
DR   InterPro; IPR037064; Formiminotransferase_N_sf.
DR   InterPro; IPR022384; FormiminoTrfase_cat_dom_sf.
DR   InterPro; IPR036178; Formintransfe-cycloase-like_sf.
DR   NCBIfam; TIGR02024; FtcD; 1.
DR   PANTHER; PTHR12234:SF0; FORMIMIDOYLTRANSFERASE-CYCLODEAMINASE; 1.
DR   PANTHER; PTHR12234; FORMIMINOTRANSFERASE-CYCLODEAMINASE; 1.
DR   Pfam; PF02971; FTCD; 1.
DR   Pfam; PF04961; FTCD_C; 1.
DR   Pfam; PF07837; FTCD_N; 1.
DR   SMART; SM01221; FTCD; 1.
DR   SMART; SM01222; FTCD_N; 1.
DR   SUPFAM; SSF55116; Formiminotransferase domain of formiminotransferase-cyclodeaminase; 2.
DR   SUPFAM; SSF101262; Methenyltetrahydrofolate cyclohydrolase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Folate-binding {ECO:0000256|ARBA:ARBA00022954};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Histidine metabolism {ECO:0000256|ARBA:ARBA00022808};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCZ75778.1}.
FT   DOMAIN          4..184
FT                   /note="Formiminotransferase N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01222"
FT   DOMAIN          185..350
FT                   /note="Formiminotransferase C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01221"
SQ   SEQUENCE   565 AA;  60737 MW;  23CB6FAFB3E27632 CRC64;
     MEKRIVECVP NFSEGRDKAV IDRIVSAIET SGGVKVLDVD PGEATNRTVV TFVGSPEAVV
     EAAFAGVKKA AELIDMRKHK GAHPRMGATD VLPLIPIAGI TLEECAELAR KLAERIAGEL
     HVPTYCYEAA AFTPRRRNLA VCREGEYEAL PEKLAHEESA PDFGARPFDE GVARTGATTV
     GARDFLIAVN FNLNTTSTRR ANAIAFDVRE KGRPVREGNP ITGKVVRDAD GNPLMRPGTL
     RATKAIGWFI EEYGIAQVSM NITDIAVTPL HVAFDEVCRK ADARGVRVTG TEIVGLVPKR
     ALLEAGRYFL RKQQRSAGIA EEEIVRIAVK SMGLDDLKPF DPKEKVIEYL LEAEDQKKRL
     IDMTCKGFAE ETASESPAPG GGSIAAYMGA LGAALGTMVA NLSSHKAGWD DRWEEFSGWA
     EKGQALLREL LHLVDEDTAA FNRIMDVFAM PKSTDEEKAA RSAALQAATL YATQVPLRTM
     KTAFEVFAIV RAMAAEGNPN SVSDAGVGAL AARSAVLGAC LNVKINAAGL KDRAAADALV
     AEANSVAAAA ERAEREVLEI VERKI
//
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