CMOA_HAEIN
ID CMOA_HAEIN Reviewed; 241 AA.
AC P43985; P43986;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Carboxy-S-adenosyl-L-methionine synthase {ECO:0000255|HAMAP-Rule:MF_01589};
DE Short=Cx-SAM synthase {ECO:0000255|HAMAP-Rule:MF_01589};
DE EC=2.1.3.- {ECO:0000255|HAMAP-Rule:MF_01589};
GN Name=cmoA {ECO:0000255|HAMAP-Rule:MF_01589}; OrderedLocusNames=HI_0319;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP SEQUENCE REVISION.
RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOSELENOCYSTEINE, AND SUBUNIT.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=11746687; DOI=10.1002/prot.10004;
RA Lim K., Zhang H., Tempczyk A., Bonander N., Toedt J., Howard A.,
RA Eisenstein E., Herzberg O.;
RT "Crystal structure of YecO from Haemophilus influenzae (HI0319) reveals a
RT methyltransferase fold and a bound S-adenosylhomocysteine.";
RL Proteins 45:397-407(2001).
CC -!- FUNCTION: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to
CC carboxy-S-adenosyl-L-methionine (Cx-SAM). {ECO:0000255|HAMAP-
CC Rule:MF_01589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate +
CC carboxy-S-adenosyl-L-methionine + H2O; Xref=Rhea:RHEA:51692,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:134278; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01589};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01589,
CC ECO:0000269|PubMed:11746687}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cx-SAM synthase family. {ECO:0000255|HAMAP-Rule:MF_01589}.
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DR EMBL; L42023; AAC21983.1; -; Genomic_DNA.
DR PIR; C64006; C64006.
DR RefSeq; NP_438485.1; NC_000907.1.
DR RefSeq; WP_005694346.1; NC_000907.1.
DR PDB; 1IM8; X-ray; 2.20 A; A/B=1-241.
DR PDBsum; 1IM8; -.
DR AlphaFoldDB; P43985; -.
DR SMR; P43985; -.
DR STRING; 71421.HI_0319; -.
DR DrugBank; DB03423; S-Adenosyl-L-Homoselenocysteine.
DR EnsemblBacteria; AAC21983; AAC21983; HI_0319.
DR KEGG; hin:HI_0319; -.
DR PATRIC; fig|71421.8.peg.337; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_078475_0_0_6; -.
DR OMA; MIELYYL; -.
DR PhylomeDB; P43985; -.
DR BioCyc; HINF71421:G1GJ1-336-MON; -.
DR EvolutionaryTrace; P43985; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01589; Cx_SAM_synthase; 1.
DR InterPro; IPR005271; CmoA.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43861:SF2; PTHR43861:SF2; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR PIRSF; PIRSF006325; MeTrfase_bac; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00740; TIGR00740; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..241
FT /note="Carboxy-S-adenosyl-L-methionine synthase"
FT /id="PRO_0000169084"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589,
FT ECO:0000305|PubMed:11746687"
FT BINDING 63..65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589,
FT ECO:0000305|PubMed:11746687"
FT BINDING 88..89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589,
FT ECO:0000305|PubMed:11746687"
FT BINDING 116..117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589,
FT ECO:0000305|PubMed:11746687"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589,
FT ECO:0000305|PubMed:11746687"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01589"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:1IM8"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:1IM8"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:1IM8"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1IM8"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1IM8"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:1IM8"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 170..186
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:1IM8"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:1IM8"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:1IM8"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:1IM8"
SQ SEQUENCE 241 AA; 27372 MW; 08743633A3E853F8 CRC64;
MVKDTLFSTP IAKLGDFIFD ENVAEVFPDM IQRSVPGYSN IITAIGMLAE RFVTADSNVY
DLGCSRGAAT LSARRNINQP NVKIIGIDNS QPMVERCRQH IAAYHSEIPV EILCNDIRHV
EIKNASMVIL NFTLQFLPPE DRIALLTKIY EGLNPNGVLV LSEKFRFEDT KINHLLIDLH
HQFKRANGYS ELEVSQKRTA LENVMRTDSI ETHKVRLKNV GFSQVELWFQ CFNFGSMIAV
K
