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Database: UniProt
Entry: A3VMM8_9RHOB
LinkDB: A3VMM8_9RHOB
Original site: A3VMM8_9RHOB 
ID   A3VMM8_9RHOB            Unreviewed;       327 AA.
AC   A3VMM8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
GN   ORFNames=RB2654_18218 {ECO:0000313|EMBL:EAQ10481.1};
OS   Maritimibacter alkaliphilus HTCC2654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ10481.1, ECO:0000313|Proteomes:UP000002931};
RN   [1] {ECO:0000313|EMBL:EAQ10481.1, ECO:0000313|Proteomes:UP000002931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ10481.1,
RC   ECO:0000313|Proteomes:UP000002931};
RX   PubMed=20729358; DOI=10.1128/JB.00873-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT   alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT   genera.";
RL   J. Bacteriol. 192:5552-5553(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-
CC         methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH;
CC         Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.54;
CC         Evidence={ECO:0000256|ARBA:ARBA00034420};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19823;
CC         Evidence={ECO:0000256|ARBA:ARBA00034420};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU003862};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway. {ECO:0000256|ARBA:ARBA00034478}.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU003862}.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC       {ECO:0000256|ARBA:ARBA00006743, ECO:0000256|RuleBase:RU003862}.
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:EAQ10481.1}.
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DR   EMBL; AAMT01000035; EAQ10481.1; -; Genomic_DNA.
DR   RefSeq; WP_008334253.1; NZ_VNHV01000004.1.
DR   AlphaFoldDB; A3VMM8; -.
DR   STRING; 314271.RB2654_18218; -.
DR   eggNOG; COG0685; Bacteria.
DR   HOGENOM; CLU_057297_2_0_5; -.
DR   OrthoDB; 9803687at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002931; Unassembled WGS sequence.
DR   GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA.
DR   GO; GO:0006555; P:methionine metabolic process; IEA:InterPro.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00537; MTHFR; 1.
DR   Gene3D; 3.20.20.220; -; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003171; Mehydrof_redctse-like.
DR   PANTHER; PTHR45754; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR45754:SF3; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF02219; MTHFR; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003862};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003862};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003862};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002931}.
SQ   SEQUENCE   327 AA;  35506 MW;  D667CFC316CA5997 CRC64;
     MSMFYSDPNA IRPYEPIPEG HKAGSVLERT LRAGEFAVTS ELNPPDSADP EDVFAAAKPL
     AEVTDAINAT DASGANCHMS SIGICSLLTR TGHGSVYQIS CRDRNRIAIQ GDVLGAAAMG
     VRNVLCLTGD DVGAGDQPGA KPVFDLDSVS LIRLIKTMRD EGRFLSGREI AKPPRLFIGA
     AENPCVDPVD YRADRLAKKV EAGADFIQTN YIFDIPRFER FMERVRDMGL DKRVFILAGV
     GPLASAKAAR WMRSNVPGIH IPDSVIDRLA KAEKPGDEGR RICVELIQQV KDIAGVSGVH
     IMAYRREHLV ADILREAGIA RPQKQSA
//
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