ID A0A0A2E0V8_9PORP Unreviewed; 567 AA.
AC A0A0A2E0V8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=HQ37_02050 {ECO:0000313|EMBL:KGN71257.1};
OS Porphyromonas sp. COT-239 OH1446.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN71257.1, ECO:0000313|Proteomes:UP000030150};
RN [1] {ECO:0000313|EMBL:KGN71257.1, ECO:0000313|Proteomes:UP000030150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. COT-239_OH1446 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN71257.1}.
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DR EMBL; JRAO01000010; KGN71257.1; -; Genomic_DNA.
DR RefSeq; WP_036879634.1; NZ_JRAO01000010.1.
DR AlphaFoldDB; A0A0A2E0V8; -.
DR STRING; 1515613.HQ37_02050; -.
DR eggNOG; COG3404; Bacteria.
DR eggNOG; COG3643; Bacteria.
DR OrthoDB; 9773217at2; -.
DR UniPathway; UPA00379; UER00555.
DR Proteomes; UP000030150; 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:UP000030150};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGN71257.1}.
FT DOMAIN 6..186
FT /note="Formiminotransferase N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01222"
FT DOMAIN 187..352
FT /note="Formiminotransferase C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01221"
FT REGION 213..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 62025 MW; 36A452CE09484F94 CRC64;
MAREKQIVEC VPNISEGRNK EVIKQVTDEI ERVKGIKLLD VDPGEATNRT VITFVGTPDQ
VMEAAFRCVK RASELIDMRH HHGAHPRMGA TDVCPFIPVS GITLEECAAL SRQLAERIAS
ELHIPCYCYE AAARRPERKN LAVCRKGEYE GLPERMTIES EAPDFGARPW DEGVARTGCT
AVGARDFLIA ANYNLNTTST RRANAIAFDV REKGRPQREG GSPVGKPMLD AEGNPIMIPG
TLPGTKAIGW YIDEYGIAQV SMNITDMHTT PLHVAFDEVC RCAQRRGVRV TGTEIVGLIP
KRTLIDAGKY FLRKQNRSTG IPEEDIIKIA VKSMGLDDLK EFNTREKVIE FLLEDEERKP
MLIDLTVKGF ADETSRESPA PGGGTISAYM GALGAALGTM VANLSSHKAG WDARWEEFSH
WADKGQQLQH ELMVLVDEDT EAFNRIMEAF GLPKGTPEEK AARTAAIQEA TLFATQVPLH
TMQASYKVFE LCRAMAEEGN PNSVSDAGVG VLAARAAVLG AGLNVKINAS GLKDRETADK
LVAEANELIA KANEEEAAIL KIVESKL
//
