(data stored in SCRATCH zone)

SWISSPROT: A0KFD9_AERHH

ID   A0KFD9_AERHH            Unreviewed;      1227 AA.
AC   A0KFD9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 102.
DE   RecName: Full=Methionine synthase {ECO:0000256|PIRNR:PIRNR000381};
DE            EC=2.1.1.13 {ECO:0000256|PIRNR:PIRNR000381};
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000256|PIRNR:PIRNR000381};
GN   Name=metH {ECO:0000313|EMBL:ABK39635.1};
GN   OrderedLocusNames=AHA_0432 {ECO:0000313|EMBL:ABK39635.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39635.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39635.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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|PIRNR:PIRNR000381}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-methionine;
CC         Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000381};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000381-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381-
CC       1};
CC   -!- COFACTOR:
CC       Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000381,
CC         ECO:0000256|PIRSR:PIRSR000381-2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetH route): step
CC       1/1. {ECO:0000256|PIRNR:PIRNR000381}.
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DR   EMBL; CP000462; ABK39635.1; -; Genomic_DNA.
DR   RefSeq; WP_011704406.1; NC_008570.1.
DR   RefSeq; YP_854961.1; NC_008570.1.
DR   STRING; 380703.AHA_0432; -.
DR   EnsemblBacteria; ABK39635; ABK39635; AHA_0432.
DR   GeneID; 4488402; -.
DR   KEGG; aha:AHA_0432; -.
DR   PATRIC; fig|380703.7.peg.421; -.
DR   eggNOG; ENOG4105C3R; Bacteria.
DR   eggNOG; COG0646; LUCA.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251409; -.
DR   KO; K00548; -.
DR   OMA; ADCIAMS; -.
DR   BioCyc; AHYD380703:G1G7B-433-MONOMER; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd02069; methionine_synthase_B12_BD; 1.
DR   Gene3D; 1.10.1240.10; -; 1.
DR   Gene3D; 3.10.196.10; -; 1.
DR   Gene3D; 3.20.20.20; -; 1.
DR   Gene3D; 3.20.20.330; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   InterPro; IPR033706; Met_synthase_B12-bd.
DR   InterPro; IPR011822; MetH.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
DR   InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   Pfam; PF02965; Met_synt_B12; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF000381; MetH; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF47644; SSF47644; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   SUPFAM; SSF56507; SSF56507; 1.
DR   SUPFAM; SSF82282; SSF82282; 1.
DR   TIGRFAMs; TIGR02082; metH; 1.
DR   PROSITE; PS50974; ADOMET_ACTIVATION; 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   4: Predicted;
DR   PRODOM; A0KFD9.
DR   SWISS-2DPAGE; A0KFD9.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Cobalamin {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Cobalt {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-
KW   1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00333, ECO:0000313|EMBL:ABK39635.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00333, ECO:0000313|EMBL:ABK39635.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1,
KW   ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN        9    329       Hcy-binding. {ECO:0000259|PROSITE:
FT                                PS50970}.
FT   DOMAIN      360    624       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      653    747       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      749    884       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      900   1227       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      837    838       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION     1193   1194       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   COILED      974    994       {ECO:0000256|SAM:Coils}.
FT   METAL       251    251       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       314    314       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       315    315       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       762    762       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     807    807       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     950    950       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING    1138   1138       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING    1142   1142       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   1227 AA;  135105 MW;  87996AA086223C8D CRC64;
     MSNKKSDVTN KLEACLKERI LIIDGAMGTM IQGYKLGEAD YRGARFADWH TDIKGNNDLL
     VLTRPAVIRE IHEQYCAAGA DILETNTFNA TRIAMADYEM EEFSAEINCE AARLARAVAD
     EWTAKEPHKP RFVAGVLGPT NRTASISPDV NDPGKRNVTY DQLVAAYTES THALIEGGAD
     IILIETIFDT LNAKAAAFAV EGVFEALGYS LPVMISGTIT DASGRTLSGQ TTEAFYHSLR
     HVKPVSFGLN CALGPDELRQ YVEELSRISE THVSAHPNAG LPNAFGEYDL DAVEMAEHIR
     EWAASGFLNL VGGCCGTTPT HIRAMADAVA GIKPRALPEL PVACRLSGLE PLIITPESMF
     VNVGERTNVT GSAKFKRLIK EGLYDEALDV AKQQVESGAQ IIDINMDEGM LDAEAAMVRF
     LNLIAGEPDI ARVPVMIDSS KWEVLEAGLK CVQGKPVVNS ISMKEGEEKF IQQARLLRRY
     GAAVIVMAFD EVGQADTRAR KFEICQRAYR ILVDRVGFPP EDIIFDPNIF AVATGIDEHN
     NYAVDFIDAV KDIKQNLPHA MISGGVSNVS FSFRGNEPVR EAIHAVFLYH AIQNGMDMGI
     VNAGQLAIYE DIPSDLKEKV EAVVLNLNPD ATEALLAIAE RYRGGGAQTE DPRDQAWRSW
     PVGKRLEHAL VKGITDFIEE DTEEARSKAE KPLHVIEGPL MDGMNVVGDL FGAGKMFLPQ
     VVKSARVMKR AVAYLQPYIE AEKSGGSSNG KIVMATVKGD VHDIGKNIVG VVLQCNNYEI
     VDLGVMVSCE TILKTAREVN ADIIGLSGLI TPSLDEMVHV AKEMERQGFK LPLLIGGATT
     SKAHTAVKIE QNYSEPVVYV SNASRAVGVA QSLLSPELKP AFVARIDKEY EIAREQHARK
     QPRSKPVSLA HARANRHQLD WVGYQPPKPR EPGVQTFEDV PVSVLRPYID WTPFFLSWEL
     AGKFPRILED EVVGEEATRL YADANAMLDQ LEQDRSVRCA GIIGLFPANA VGDSIEVYTD
     ESRREVRKVL HHLRQQSEKQ GFPNYCLADY VAPKESGKPD WIGAFAVTGG IGEEAIAKAY
     KAEHDDYNAI LIQAVCDRLA EAFAEYLHEQ VRKVHWGYAP NEALSNEELI RENYRGIRPA
     PGYPACPEHT EKGSIWELLG VEQAIGMKLT ESYAMWPGAA VSGWYFSHPD SKYFAVAQIQ
     QDQVEDYAQR KGMTLAEAER WLGPNLH
//

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