(data stored in SCRATCH zone)

SWISSPROT: D7A337_STAND

ID   D7A337_STAND            Unreviewed;       420 AA.
AC   D7A337;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00051};
DE            Short=SHMT {ECO:0000256|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase {ECO:0000256|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.1 {ECO:0000256|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051};
GN   OrderedLocusNames=Snov_0422 {ECO:0000313|EMBL:ADH87755.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87755.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87755.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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.
CC       {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine +
CC         H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine;
CC         Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453;
CC         EC=2.1.2.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00051,
CC         ECO:0000256|PIRSR:PIRSR000412-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|HAMAP-
CC       Rule:MF_00051}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00051}.
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DR   EMBL; CP002026; ADH87755.1; -; Genomic_DNA.
DR   RefSeq; WP_013165260.1; NC_014217.1.
DR   STRING; 639283.Snov_0422; -.
DR   EnsemblBacteria; ADH87755; ADH87755; Snov_0422.
DR   KEGG; sno:Snov_0422; -.
DR   eggNOG; ENOG4108QGD; Bacteria.
DR   eggNOG; COG0112; LUCA.
DR   HOGENOM; HOG000239404; -.
DR   OMA; GARYYCG; -.
DR   OrthoDB; 861782at2; -.
DR   BioCyc; SNOV639283:G1GLM-427-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00378; SHMT; 1.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; PTHR11680; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
DR   PRODOM; D7A337.
DR   SWISS-2DPAGE; D7A337.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:ADH87755.1};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00051,
KW   ECO:0000256|PIRSR:PIRSR000412-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00051,
KW   ECO:0000313|EMBL:ADH87755.1}.
FT   DOMAIN       14    389       SHMT. {ECO:0000259|Pfam:PF00464}.
FT   REGION      129    131       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      39     39       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      61     61       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      68     68       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      69     69       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     103    103       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     180    180       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     208    208       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     240    240       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     366    366       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     234    234       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051,
FT                                ECO:0000256|PIRSR:PIRSR000412-50}.
SQ   SEQUENCE   420 AA;  43972 MW;  534AE17C5D32ED6E CRC64;
     MSTLHAGYFT EGLDADPELA AALRGELKRQ QDGIELIASE NIVSRLVLEA QGSVLTNKTV
     EGLPYARYYG GAEFADAIEA LAVERAKKLF NCRFANVQPH SGSNANAGVF LGLLKLGDTI
     LSMNTAAGGH ISHGHPATLT GRDYRIVPYG VSRETERIEL DELRTLALDH APKLIVAGGS
     AYPPAIDFAG MRAIADEVGA LFMVDMAHFA GLVATGLYPH PFPHAHVVTS TTYKSLRGAR
     GGIVLWNDAS LNDRINYGIF PGVQGSVMMH AVAGKAACFG EALKPEFHAY NEAVLANARA
     MAAALATEGL RIVGGGTDCG LMLVDLSPLG VTGDIAAKAL EKAGLAVNKN LVPFDPRPPE
     APSGLRLSSN AGTARGFGIA EFETIAGWIA RVVKAPADAA AIAAVRAQVT SLCASFPIYA
//

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