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Database: UniProt
Entry: F2LVY3_HIPMA
LinkDB: F2LVY3_HIPMA
Original site: F2LVY3_HIPMA 
ID   F2LVY3_HIPMA            Unreviewed;       806 AA.
AC   F2LVY3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Methionine synthase {ECO:0000256|ARBA:ARBA00013998};
DE            EC=2.1.1.13 {ECO:0000256|ARBA:ARBA00012032};
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000256|ARBA:ARBA00031040};
GN   OrderedLocusNames=Hipma_0948 {ECO:0000313|EMBL:AEA33917.1};
OS   Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2).
OC   Bacteria; Campylobacterota; Desulfurellia; Desulfurellales; Hippeaceae;
OC   Hippea.
OX   NCBI_TaxID=760142 {ECO:0000313|EMBL:AEA33917.1, ECO:0000313|Proteomes:UP000008139};
RN   [1] {ECO:0000313|EMBL:AEA33917.1, ECO:0000313|Proteomes:UP000008139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700847 / DSM 10411 / MH2
RC   {ECO:0000313|Proteomes:UP000008139};
RX   PubMed=21886857;
RA   Huntemann M., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Ovchinikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Rohde M., Spring S., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Mavromatis K.;
RT   "Complete genome sequence of the thermophilic sulfur-reducer Hippea
RT   maritima type strain (MH(2)).";
RL   Stand. Genomic Sci. 4:303-311(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700847 / DSM 10411 / MH2
RC   {ECO:0000313|Proteomes:UP000008139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Hippea maritima DSM 10411.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl-
CC       cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and
CC       methionine. Subsequently, remethylates the cofactor using
CC       methyltetrahydrofolate. {ECO:0000256|ARBA:ARBA00025552}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58199; EC=2.1.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001700};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|PROSITE-ProRule:PRU00333};
CC   -!- COFACTOR:
CC       Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000256|ARBA:ARBA00001956};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005178}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
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DR   EMBL; CP002606; AEA33917.1; -; Genomic_DNA.
DR   RefSeq; WP_013681958.1; NC_015318.1.
DR   AlphaFoldDB; F2LVY3; -.
DR   STRING; 760142.Hipma_0948; -.
DR   KEGG; hmr:Hipma_0948; -.
DR   eggNOG; COG0646; Bacteria.
DR   eggNOG; COG1410; Bacteria.
DR   HOGENOM; CLU_004914_0_2_7; -.
DR   InParanoid; F2LVY3; -.
DR   OrthoDB; 9803687at2; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000008139; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd02070; corrinoid_protein_B12-BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR   Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   InterPro; IPR017215; MetH_bac.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF037472; DHPS_mtfrase; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   SUPFAM; SSF47644; Methionine synthase domain; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
DR   PROSITE; PS50970; HCY; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000008139};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          1..286
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   DOMAIN          317..561
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
FT   DOMAIN          592..685
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51337"
FT   DOMAIN          687..806
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   806 AA;  88553 MW;  0DBC9A5840E32A31 CRC64;
     MRNFREELGR KILILDGAMG TQLQEKGILK TGSCPDYLNV THPKEIGEIH KTYLDAGADI
     IVTNTFGANP IKLEEFNLQD KVYQINYEAV RIAKEVVKDK GFVSLSIGPT GKFIEPVGEE
     NFDYIKDIFK KQVRPAVDAD VDLFSLETFM DIKELKAAII AIREITDKPI IAMMTFAEDG
     RTILGTSPEV FAKTIEPMEV DVIGANCSVG PDLLNEFVKK MAQVTDKPLI IQPNAGIPRL
     VNGKTIFPVG AEEFASYAND FKEYAAIVAG CCGTGPEHIK LLAEKLKGKP VKKRTIQKAT
     VLTSRSQMVE IGYSRPVVFI GERLNPTGKK HLKEQLKEGK TGLYRKEAIE QVEHGAMVLD
     INVGVPMIDE PTTMKKCVLA VESVVSVPLV IDSSNIEALE AGLKAADGKV LINSVNGSQE
     SMEAILPLAK KYGAAILALL LDETGIPETA EDRLKILDKI VKNAKELGIK EEDIVADALA
     LTIGSDKKRA LETLRAIKLI KEKYGITTIL GLSNVSFGLP NRKLINSSFM AMAIYNGLDS
     AIVNPYDELL WQIKYASDLI VDRDKDSSIY INNSSDITLK NKTTDNAKLE LIKSPFDKGT
     LEDKLFMCVI EGNEEEIELL TKQALKNKEP LKISNEILIP ALDAVGKLYD KGIYFLPQMI
     KSANAMKKAF NILKEIIKKK ATKQKTGKTI VMATVKGDIH DIGKNIVSLL LETNGFEVVD
     LGKNVDDETI LKAIEEYHAD AVGLSALMTT TMINMKNVID EIKMKGLNVK IMVGGAAVTE
     EFAKKIGADM YAKDAIEAVR LAKENV
//
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