FHCD_METEA
ID FHCD_METEA Reviewed; 311 AA.
AC Q49118; C5B136;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Formyltransferase/hydrolase complex subunit D {ECO:0000303|PubMed:12123819};
DE Short=Ftr complex {ECO:0000303|PubMed:12123819};
DE EC=2.3.1.101 {ECO:0000255|HAMAP-Rule:MF_00579, ECO:0000269|PubMed:11532013};
DE AltName: Full=Formylmethanofuran--tetrahydromethanopterin formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579, ECO:0000303|PubMed:11532013};
DE Short=Ftr {ECO:0000255|HAMAP-Rule:MF_00579, ECO:0000303|PubMed:11532013};
DE AltName: Full=H4MPT formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579};
GN Name=ffsA {ECO:0000255|HAMAP-Rule:MF_00579};
GN Synonyms=fhcD {ECO:0000303|PubMed:9651254};
GN OrderedLocusNames=MexAM1_META1p1756;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9651254; DOI=10.1126/science.281.5373.99;
RA Chistoserdova L.V., Vorholt J.A., Thauer R.K., Lidstrom M.E.;
RT "C1 transfer enzymes and coenzymes linking methylotrophic bacteria and
RT methanogenic Archaea.";
RL Science 281:99-102(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [3]
RP PROTEIN SEQUENCE OF 2-16, FUNCTION AS A FORMYLTRANSFERASE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=11532013; DOI=10.1046/j.1432-1327.2001.02401.x;
RA Pomper B.K., Vorholt J.A.;
RT "Characterization of the formyltransferase from Methylobacterium extorquens
RT AM1.";
RL Eur. J. Biochem. 268:4769-4775(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=12123819; DOI=10.1016/s0014-5793(02)02962-9;
RA Pomper B.K., Saurel O., Milon A., Vorholt J.A.;
RT "Generation of formate by the formyltransferase/hydrolase complex (Fhc)
RT from Methylobacterium extorquens AM1.";
RL FEBS Lett. 523:133-137(2002).
CC -!- FUNCTION: Involved in the transformation of 5-formyl
CC tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and
CC formate via the intermediate formylmethanofuran (formyl-MFR). Catalyzes
CC the transfer of a formyl group from 5-formyl-H(4)MPT to MFR to produce
CC tetrahydromethanopterin (H(4)MPT) and formyl-MFR, which is then
CC hydrolyzed to formate and MFR. {ECO:0000269|PubMed:11532013,
CC ECO:0000269|PubMed:12123819}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydromethanopterin + H(+) + N-formylmethanofuran
CC = methanofuran + N(5)-formyl-5,6,7,8-tetrahydromethanopterin;
CC Xref=Rhea:RHEA:18061, ChEBI:CHEBI:15378, ChEBI:CHEBI:57727,
CC ChEBI:CHEBI:58018, ChEBI:CHEBI:58103, ChEBI:CHEBI:58151;
CC EC=2.3.1.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00579,
CC ECO:0000269|PubMed:11532013, ECO:0000269|PubMed:12123819};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for H(4)MPT {ECO:0000269|PubMed:11532013};
CC KM=50 uM for formyl-MFR {ECO:0000269|PubMed:11532013};
CC Vmax=80 umol/min/mg enzyme {ECO:0000269|PubMed:11532013};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:11532013};
CC -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC formaldehyde (H(4)MPT route): step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00579}.
CC -!- SUBUNIT: Homotetramer (By similarity). Octaheteromer. Part of the
CC formyltransferase/hydrolase complex fhc; composed of FhcA, FhcB, FhcC
CC and FhcD (PubMed:11532013, PubMed:12123819). {ECO:0000255|HAMAP-
CC Rule:MF_00579, ECO:0000269|PubMed:11532013,
CC ECO:0000269|PubMed:12123819}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00579}.
CC -!- SIMILARITY: Belongs to the FTR family. {ECO:0000255|HAMAP-
CC Rule:MF_00579}.
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DR EMBL; AF032114; AAC26972.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS39600.1; -; Genomic_DNA.
DR PIR; T45153; T45153.
DR RefSeq; WP_003597588.1; NC_012808.1.
DR AlphaFoldDB; Q49118; -.
DR SMR; Q49118; -.
DR STRING; 272630.MexAM1_META1p1756; -.
DR EnsemblBacteria; ACS39600; ACS39600; MexAM1_META1p1756.
DR KEGG; mea:Mex_1p1756; -.
DR eggNOG; COG2037; Bacteria.
DR HOGENOM; CLU_081314_0_0_5; -.
DR OMA; VIMCPAE; -.
DR OrthoDB; 895502at2; -.
DR BioCyc; MetaCyc:MON-4065; -.
DR UniPathway; UPA00562; UER00704.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030270; F:formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.70.520; -; 2.
DR HAMAP; MF_00579; FTR; 1.
DR InterPro; IPR014053; ForMFR_H4MPT_ForTrfase.
DR InterPro; IPR002770; ForMFR_H4MPT_ForTrfase_C.
DR InterPro; IPR023447; ForMFR_H4MPT_ForTrfase_fd-like.
DR InterPro; IPR022667; ForMFR_H4MPT_ForTrfase_N.
DR Pfam; PF01913; FTR; 1.
DR Pfam; PF02741; FTR_C; 1.
DR PIRSF; PIRSF006414; Ftr_formyl_trnsf; 1.
DR SUPFAM; SSF55112; SSF55112; 2.
DR TIGRFAMs; TIGR03119; one_C_fhcD; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Direct protein sequencing;
KW One-carbon metabolism; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11532013"
FT CHAIN 2..311
FT /note="Formyltransferase/hydrolase complex subunit D"
FT /id="PRO_0000138124"
SQ SEQUENCE 311 AA; 32374 MW; F25FBE3918729428 CRC64;
MSDFTLNGIK VEDTFAEAFD VAGTAIIVTN DTPKWAMIAA TVMTGFATSV IGCGAEAGID
AELSPDETPD GRPGVRILLF GFEPNGLKDQ LLKRVGQCIL TCPGTACFAG VEGPTKIKLG
GAIRYFGDGF AVAKRLPDHE GKMRRYWRIP VMDGEFLCED SVRAVDGAVG GGNLLFLGRK
HADTLIVAEI AVEAAKAIPG AILPFPGGIV RSGSKVGGRT KGMMASTNDA YCPTLKGRAG
SALPPECGVV LEIVIDALTS AAVAESMRAA LHAATEIGAQ HGLVAVTAGN YGGNLGRHHY
HLRDLLEKPA A
