ID GLYA_ALKMQ Reviewed; 410 AA.
AC A6TQQ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 01-MAY-2013, entry version 44.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA; OrderedLocusNames=Amet_2365;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Ye Q.,
RA Zhou J., Fields M., Richardson P.;
RT "Complete sequence of Alkaliphilus metalliredigens QYMF.";
RL Submitted (JUN-2007) 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: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC from L-serine: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the SHMT family.
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DR EMBL; CP000724; ABR48519.1; -; Genomic_DNA.
DR RefSeq; YP_001320178.1; NC_009633.1.
DR ProteinModelPortal; A6TQQ1; -.
DR SMR; A6TQQ1; 6-404.
DR STRING; 293826.Amet_2365; -.
DR EnsemblBacteria; ABR48519; ABR48519; Amet_2365.
DR GeneID; 5312437; -.
DR KEGG; amt:Amet_2365; -.
DR eggNOG; COG0112; -.
DR HOGENOM; HOG000239403; -.
DR KO; K00600; -.
DR OMA; HPERIDE; -.
DR ProtClustDB; PRK00011; -.
DR BioCyc; AMET293826:GI5P-2503-MONOMER; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
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:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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 InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR PANTHER; PTHR11680; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW One-carbon metabolism; Pyridoxal phosphate; Transferase.
FT CHAIN 1 410 Serine hydroxymethyltransferase.
FT /FTId=PRO_1000057362.
FT REGION 123 125 Substrate binding (By similarity).
FT REGION 351 353 Substrate binding (By similarity).
FT BINDING 33 33 Pyridoxal phosphate (By similarity).
FT BINDING 53 53 Pyridoxal phosphate (By similarity).
FT BINDING 55 55 Substrate (By similarity).
FT BINDING 62 62 Substrate (By similarity).
FT BINDING 63 63 Pyridoxal phosphate (By similarity).
FT BINDING 119 119 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 174 174 Pyridoxal phosphate (By similarity).
FT BINDING 202 202 Pyridoxal phosphate (By similarity).
FT BINDING 227 227 Pyridoxal phosphate (By similarity).
FT BINDING 234 234 Pyridoxal phosphate (By similarity).
FT BINDING 259 259 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 359 359 Pyridoxal phosphate (By similarity).
FT MOD_RES 228 228 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 410 AA; 45223 MW; 55F9893A45D63B94 CRC64;
MNFDTLKKFD EEIYEVIQKE TKRQRGSIEL IASENFVTTA VMEAMGSQLT NKYAEGYPDK
RYYGGCEEVD VAENLARNRL KKLFNAEHAN VQPHSGANAN IGVYFATLEP GDTVLGMNLS
HGGHLTHGSP VNISGAYYNF VAYGVDSVTH RIDYEEVMRV AQEAKPKMIV AGASAYPRAI
DFKKFREIAD AVGAYLMVDM AHIAGLVAVG LHQNPCEYAD FVTTTTHKTL RGPRGGAILC
KEKYAKIIDK AIFPGLQGGP LMHVIAAKAV AFKEALEPGF KAYQEQVIKN AKALGEELKK
QGFDLVSDGT DTHLLLIDLR NKNITGKDAE RLFDEVGITV NKNTIPFDPQ SPFVTSGIRI
GTPAVTTRGM KEEEMKKIAG VMNIIIDHPE KVSEAQKVVD ELCNQFKLYE
//
