ID R5QNV7_9FIRM Unreviewed; 812 AA.
AC R5QNV7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Methylenetetrahydrofolate reductase {ECO:0000313|EMBL:CCZ28004.1};
GN ORFNames=BN526_00446 {ECO:0000313|EMBL:CCZ28004.1};
OS Firmicutes bacterium CAG:194.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263008 {ECO:0000313|EMBL:CCZ28004.1, ECO:0000313|Proteomes:UP000018384};
RN [1] {ECO:0000313|EMBL:CCZ28004.1, ECO:0000313|Proteomes:UP000018384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:194 {ECO:0000313|Proteomes:UP000018384};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777}.
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:CCZ28004.1}.
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DR EMBL; CAZT010000028; CCZ28004.1; -; Genomic_DNA.
DR AlphaFoldDB; R5QNV7; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000018384; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00537; MTHFR; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR InterPro; IPR003171; Mehydrof_redctse-like.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR PANTHER; PTHR11103:SF18; HOMOCYSTEINE S-METHYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR11103; SLR1189 PROTEIN; 1.
DR Pfam; PF13419; HAD_2; 1.
DR Pfam; PF02219; MTHFR; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR PROSITE; PS50970; HCY; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018384};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 212..496
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 481
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 812 AA; 90079 MW; 58583486DCBB482C CRC64;
MKQGILFDLD GTLWDSAQAV VDSWNEIIET LPDFHKLITN EDMCQLMGKT MDDIAYTYFN
TVSKERALEI LQICMDHENA YIEQHGGVLF PGLEEVLKEL SEKYDLFIVS NCQLGYIEAF
LSYHKLGKYF KDTECYGRTK RCKGDSIAIL LGRQDLEQAV YVGDIEGDFI SATQAGLPFI
HAAYGFGKVP QAVYAIRSVQ ELPAMAKKVF AKKDIRAFLH TQKLITDGAF GTYFSSICQN
GIFPERANTQ APALVKQVHE AYLSAGAQLI RTNTFAANTK TLDMGLDEVL ETIEAGFTIA
KEAAEPYRQK HPVFLAGDIG PIPGGRQEQE EQITEEYLQI ARKFVALGAD LLVFETFPNP
DQILPVIRQI RKESPIFILV QFAVNQLGYS VAGISARSLL EEAGQVTEID AAGLNCGVGP
GHMYNIIKQV SSLSGKYLSV LPNASYPKVV QDRLVFLENM DYFSDKMVEI ADLGASIIGG
CCGTNPDYIR RLVKALGEKH LRAEKPSPVH ITVKERTEQA EDHSFYAGKS GKLIAVELSP
PPSANDQKLL EAAHLLSAMH VDTVTFPDSP SGRTRADSIL MAAKVARETD LCVMPHICCR
DKNAIAIRSQ LLGAYLSDIR NALVITGDPV PSMAREDVRS VFNFDSVGLM KLVQEMNREE
FASDPFFVGG AINQNRLRLD VEINRVKRKM EHGATFFMTQ PVFTKEEIDK IRRIKEETGA
RILCGIMPLV SRKNALFIKN EMTGMCVTDE IVARFADGMS RSEGEAAGCA IAREMMALAA
DFADGYYFSI PFNRVYLLHD MTGVINESGK EK
//
