FHCA_METEA
ID FHCA_METEA Reviewed; 548 AA.
AC C5B137;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Formyltransferase/hydrolase complex Fhc subunit A;
DE Short=Ftr complex;
DE EC=3.5.1.-;
GN Name=fhcA; OrderedLocusNames=MexAM1_META1p1757;
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 [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 [2]
RP PROTEIN SEQUENCE OF 2-15, FUNCTION IN FORMALDEHYDE DEGRADATION, AND
RP 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 [3]
RP FUNCTION AS A HYDROLASE.
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 formylmethanofuran (formyl-MFR). May be catalyze the
CC hydrolysis of formylmethanofuran (formyl-MFR) to yield formate and MFR.
CC {ECO:0000269|PubMed:11532013, ECO:0000269|PubMed:12123819}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-formylmethanofuran = formate + methanofuran;
CC Xref=Rhea:RHEA:24686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:57727, ChEBI:CHEBI:58151;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC formaldehyde (H(4)MPT route): step 4/5.
CC -!- SUBUNIT: Octaheteromer. Part of the formyltransferase/hydrolase complex
CC fhc; composed of FhcA, FhcB, FhcC and FhcD.
CC {ECO:0000269|PubMed:11532013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC FwdA/FmdA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001510; ACS39601.1; -; Genomic_DNA.
DR RefSeq; WP_012752613.1; NC_012808.1.
DR AlphaFoldDB; C5B137; -.
DR SMR; C5B137; -.
DR STRING; 272630.MexAM1_META1p1757; -.
DR EnsemblBacteria; ACS39601; ACS39601; MexAM1_META1p1757.
DR KEGG; mea:Mex_1p1757; -.
DR eggNOG; COG1229; Bacteria.
DR HOGENOM; CLU_035587_0_0_5; -.
DR OMA; GEKMDIC; -.
DR OrthoDB; 1319925at2; -.
DR UniPathway; UPA00562; UER00704.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IDA:UniProtKB.
DR CDD; cd01304; FMDH_A; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR012027; Formylmethanofuran_DH_asu.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF07969; Amidohydro_3; 1.
DR PIRSF; PIRSF006453; FwdA; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03121; one_C_dehyd_A; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding;
KW One-carbon metabolism; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11532013"
FT CHAIN 2..548
FT /note="Formyltransferase/hydrolase complex Fhc subunit A"
FT /id="PRO_0000421571"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 548 AA; 58480 MW; 11F55F3F56BB04F0 CRC64;
MLTRIHGGRV VDPTAGRDAV GDVWIEDGRV VAPSERAPDQ TIDATGCVVM AGGVEVHSHI
AGGNVVMSRL LLPDLYVSES APNGHPFAHA GGSGSWIGAN YARMGYTTAV EPALPPSNAL
ATHLELADIP LLDRGGLAVL GNDDHLLQLL RDGEGKQAVR DLVQQTLAHS RGLGVKCINA
GGASAFKDGV LKLSLDDEIP CYGLSTRKIM SALLDAVEEI GVPHPLHVHC NNLGLPGADD
SLVATLEAAE GRRIHFAHAQ FYAYGVVDPE NPMTGGFRSA AERINAAMEA HPNATYDVGQ
VVFGQTVTIS LDILRQFGGR KGAKPKKWVI SAGDAEGGGV VPFLYRPRGP VSSLQWAIGL
ELMLLSSNPE RTILTTDHPN GGVFTEYPRI IHLLMDAEER AKEIATLPAI VGERSGLPKI
EREYSFSEIA QLTRSGPAKL LGLTDRGHLR EGAKADVAIY RDDKDRTAMF SRAKLVLKDG
QPIVEDGEVV AWFSGKTLSL DVEADAGMEK RAESYLQDRF GAGLDTFAVP DAAFPENTGT
FEDVACRA
