ID   M3FQ95_9ACTO            Unreviewed;       412 AA.
AC   M3FQ95;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   26-JUN-2013, entry version 3.
DE   RecName: Full=Serine hydroxymethyltransferase;
DE            Short=SHMT;
DE            Short=Serine methylase;
DE            EC=2.1.2.1;
GN   Name=glyA; ORFNames=SBD_3957;
OS   Streptomyces bottropensis ATCC 25435.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1054862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 25435;
RA   Zhang H., Zhou W., Zhuang Y., Liang X., Liu T.;
RT   "Draft Genome Sequence of Streptomyces bottropensis ATCC 25435, a
RT   Bottromycins-Producing Actinomycete.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydrofolate (THF) serving as the one-carbon
CC       carrier. This reaction serves as the major source of one-carbon
CC       groups required for the biosynthesis of purines, thymidylate,
CC       methionine, and other important biomolecules. Also exhibits THF-
CC       independent aldolase activity toward beta-hydroxyamino acids,
CC       producing glycine and aldehydes, via a retro-aldol mechanism (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the SHMT family.
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DR   EMBL; KB405078; EMF54289.1; -; Genomic_DNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:HAMAP.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:HAMAP.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00051; SHMT; 1; -.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   PANTHER; PTHR11680; PTHR11680; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Transferase.
FT   BINDING      59     59       Pyridoxal phosphate (By similarity).
FT   BINDING      61     61       Substrate (By similarity).
FT   BINDING     103    103       Pyridoxal phosphate (By similarity).
FT   BINDING     125    125       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     208    208       Pyridoxal phosphate (By similarity).
FT   BINDING     233    233       Pyridoxal phosphate (By similarity).
FT   BINDING     240    240       Pyridoxal phosphate (By similarity).
FT   BINDING     265    265       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen (By similarity).
FT   BINDING     360    360       Pyridoxal phosphate (By similarity).
FT   MOD_RES     234    234       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   412 AA;  43349 MW;  2559BCD9AEB4963D CRC64;
     MSVTPVLEAD VLRRQDPELA DVLLGEQDRQ ATTLQLVAAE NFTSPAVLAA LGSPLANKYA
     EGYPGARHHG GCEMVDVAER LAVERARSLF GAEHANVQSH SGSSAVLAAY AALLRPGDTV
     LAMGLHFGGH LTHGSPANFS GRWFDFVGYG VEAESGLIDR EQVRTLARTH RPKALVCGSI
     SYPRHIDYAF FREVADEVGA YLIVDAAHPI GLVAGGAAPN PVPYADIVCA TTHKVLRGPR
     GGMLLCGDEL AERVDRAVFP FTQGGAQMHT IAAKAVAFGE AATPAFTAYA HQVVANARVL
     ARGLAEEGLV VVTGGTDTHL LTVDPAPLGV DGRTARGRLA AAGMVLDCCA LPHDDARGLR
     LGTAALTTQG MGETEMARLA VLFAGALRDG GNGKRTREEV RELAGRFPPY PR
//