ID R5NQ11_9BACT Unreviewed; 567 AA.
AC R5NQ11;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BN783_02246 {ECO:0000313|EMBL:CCZ06270.1};
OS Odoribacter sp. CAG:788.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=1262909 {ECO:0000313|EMBL:CCZ06270.1, ECO:0000313|Proteomes:UP000018100};
RN [1] {ECO:0000313|EMBL:CCZ06270.1, ECO:0000313|Proteomes:UP000018100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:788 {ECO:0000313|Proteomes:UP000018100};
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:CCZ06270.1}.
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DR EMBL; CAZK010000010; CCZ06270.1; -; Genomic_DNA.
DR AlphaFoldDB; R5NQ11; -.
DR UniPathway; UPA00379; UER00555.
DR Proteomes; UP000018100; 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 Reference proteome {ECO:0000313|Proteomes:UP000018100};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCZ06270.1}.
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 567 AA; 61973 MW; AB94D140C1F4B716 CRC64;
MKKQLIECVP NFSEGNDMNI INQITDAMKT VEGISVIDVD PGKATNRTVV TMVGEPEPVC
EAAFRAVKKA AELIDMTKHK GAHPRFGATD VCPLVPVSNI TMEETVEYAR KLAKRIGDEL
NIPVYCYESA AYTPERKNLA TCRAGEYEAL GERLPSEKWH PDFGPRELNA WTAKTGATAV
GARNFLVAYN VNLNTTSTRR ANAIAFDVRE RGRVKREGNP VTGKKVLDEN GKQVMIPGTL
KSVKAIGWFI EEYGIAQISM NLTDISVTSV HEAFDEVCRK AADRGIRVTG SELVGVIPLQ
AMLDAGRYFL RKQQRSTGVS DKELIKIAVK SLGLDELYPF DPHKKIIEYI LEDEAGKGKK
KLIDMNLTDF ADETASESPA PGGGSISAYM GALGAALGAM VANLSSHKRG WDDRWEEFSN
WAEKGKSYQT ELIKLVDEDT NAFNKIMDAF SLPKKTDEEK AARQQAVQEA TRYATEVPFK
TMNLCYECMS VAKAMAEIGN PNSVTDAGVG ALAARAGVMG AFLNVKINAA GLEDKAFAEK
IIQEGETIAA KANQLEAEIL QIVNSKI
//
