Q7SIB6 (Q7SIB6_GEOSE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Serine hydroxymethyltransferase HAMAP MF_00051
Short name=SHMT HAMAP MF_00051
Short name=Serine methylase HAMAP MF_00051
EC=2.1.2.1 HAMAP MF_00051

Gene names

Name:

glyA HAMAP MF_00051

Organism

Geobacillus stearothermophilus (Bacillus stearothermophilus) PDB 1KKJ PDB 1KKP PDB 1KL1 PDB 1KL2

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Interconversion of serine and glycine By similarity. RuleBase RU000585 HAMAP MF_00051
Catalytic activity	5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine. RuleBase RU000585 HAMAP MF_00051
Cofactor	Pyridoxal phosphate By similarity. RuleBase RU000585 HAMAP MF_00051
Pathway	One-carbon metabolism; tetrahydrofolate interconversion. HAMAP MF_00051 One-carbon metabolism; tetrahydrofolate pathway. RuleBase RU000585
Subunit structure	Homotetramer By similarity. HAMAP MF_00051
Subcellular location	Cytoplasm By similarity HAMAP MF_00051.
Sequence similarities	Belongs to the SHMT family. RuleBase RU004104 HAMAP MF_00051

Ontologies

Keywords
Biological process	One-carbon metabolism RuleBase RU000585 HAMAP MF_00051
Cellular component	Cytoplasm HAMAP MF_00051
Ligand	Pyridoxal phosphate RuleBase RU000585 HAMAP MF_00051 PDB 1KKJ PDB 1KKP PDB 1KL1 PDB 1KL2 PDB 2VGS PDB 2VGW PDB 2VI8 PDB 2VMN PDB 2VMR PDB 2VMS PDB 2VMU PDB 2VMV PDB 2VMZ PDB 2W7D PDB 2W7E PDB 2W7H PDB 2W7I PDB 2VGV PDB 2VGU PDB 2VGT PDB 2VI9 PDB 2VIA PDB 2W7M PDB 2W7L PDB 2W7K PDB 2W7J PDB 2W7G PDB 2W7F PDB 1YJZ PDB 1YJY PDB 1YJS PDB 2VMO PDB 2VMP PDB 2VMW PDB 2VMX PDB 2VMQ PDB 2VMT PDB 2VMY PDB 2VIB
Molecular function	Transferase RuleBase RU000585 HAMAP MF_00051
Technical term	3D-structure PDB 1KKJ PDB 1KKP PDB 1KL1 PDB 1KL2 PDB 2VGS PDB 2VGW PDB 2VI8 PDB 2VMN PDB 2VMR PDB 2VMS PDB 2VMU PDB 2VMV PDB 2VMZ PDB 2W7D PDB 2W7E PDB 2W7H PDB 2W7I PDB 2VGV PDB 2VGU PDB 2VGT PDB 2VI9 PDB 2VIA PDB 2W7M PDB 2W7L PDB 2W7K PDB 2W7J PDB 2W7G PDB 2W7F PDB 1YJZ PDB 1YJY PDB 1YJS PDB 2VMO PDB 2VMP PDB 2VMW PDB 2VMX PDB 2VMQ PDB 2VMT PDB 2VMY PDB 2VIB
Gene Ontology (GO)
Biological process	L-serine metabolic process Inferred from electronic annotation. Source: InterPro glycine metabolic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	glycine hydroxymethyltransferase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Amino acid modifications
	Modified residue	226	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_00051
	Modified residue	226	1	Pyridoxal phosphate{EI1,EI10,EI11,EI12, EI13,EI14,EI15,EI16,EI17,EI18,EI19,EI20,EI8,EI9}

Sequences

	Sequence		Length	Mass (Da)
	Q7SIB6 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 345083DC0FF87BCA	FASTA	419	45,656
	10 20 30 40 50 60 MKYLPQQDPQ VFAAIEQERK RQHAKIELIA SENFVSRAVM EAQGSVLTNK YAEGYPGRRY 70 80 90 100 110 120 YGGCEYVDIV EELARERAKQ LFGAEHANVQ PHSGAQANMA VYFTVLEHGD TVLGMNLSHG 130 140 150 160 170 180 GHLTHGSPVN FSGVQYNFVA YGVDPETHVI DYDDVREKAR LHRPKLIVAA ASAYPRIIDF 190 200 210 220 230 240 AKFREIADEV GAYLMVDMAH IAGLVAAGLH PNPVPYAHFV TTTTHKTLRG PRGGMILCQE 250 260 270 280 290 300 QFAKQIDKAI FPGIQGGPLM HVIAAKAVAF GEALQDDFKA YAKRVVDNAK RLASALQNEG 310 320 330 340 350 360 FTLVSGGTDN HLLLVDLRPQ QLTGKTAEKV LDEVGITVNK NTIPYDPESP FVTSGIRIGT 370 380 390 400 410 AAVTTRGFGL EEMDEIAAII GLVLKNVGSE QALEEARQRV AALTDPTSRS AAGTMEFEA

References

[1]	"Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism." Trivedi V., Gupta A., Jala V.R., Saravanan P., Rao G.S., Rao N.A., Savithri H.S., Subramanya H.S. J. Biol. Chem. 277:17161-17169(2002) [PubMed: 11877399] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-226.
[2]	"Structure determination and biochemical studies on Bacillus stearothermophilus E53Q serine hydroxymethyltransferase and its complexes provide insights on function and enzyme memory." Rajaram V., Bhavani B.S., Kaul P., Prakash V., Appaji Rao N., Savithri H.S., Murthy M.R. FEBS J. 274:4148-4160(2007) [PubMed: 17651438] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-405, PYRIDOXAL PHOSPHATE AT LYS-226.
[3]	"Crystal Structure of S172Absshmt and its Complexes." Rajaram V., Bhavani B.S., Prakash V., Appaji Rao N., Savithri H.S., Murthy M.R.N. Submitted (NOV-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-405.
[4]	"Importance of tyrosine residues of Bacillus stearothermophilus serine hydroxymethyltransferase in cofactor binding and L-allo-Thr cleavage." Bhavani B.S., Rajaram V., Bisht S., Kaul P., Prakash V., Murthy M.R., Appaji Rao N., Savithri H.S. FEBS J. 275:4606-4619(2008) [PubMed: 18699779] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 1-405, PYRIDOXAL PHOSPHATE AT LYS-226.
[5]	"Role of Lys-226 in the catalytic mechanism of Bacillus stearothermophilus serine hydroxymethyltransferase--crystal structure and kinetic studies." Bhavani S., Trivedi V., Jala V.R., Subramanya H.S., Kaul P., Prakash V., Appaji Rao N., Savithri H.S. Biochemistry 44:6929-6937(2005) [PubMed: 15865438] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
[6]	"Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyltransferase: the role of Asn(341), Tyr(60) and Phe(351) in tetrahydrofolate binding." Pai V.R., Rajaram V., Bisht S., Bhavani B.S., Rao N.A., Murthy M.R., Savithri H.S. Biochem. J. 418:635-642(2009) [PubMed: 19046138] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 1-405, PYRIDOXAL PHOSPHATE AT LYS-226.
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KKJ	X-ray	1.93	A	1-419	[»]
1KKP	X-ray	1.93	A	1-419	[»]
1KL1	X-ray	1.93	A	1-419	[»]
1KL2	X-ray	2.70	A/B	1-419	[»]
1YJS	X-ray	2.00	A	1-419	[»]
1YJY	X-ray	2.25	A	1-419	[»]
1YJZ	X-ray	2.10	A	1-419	[»]
2VGS	X-ray	2.00	A	1-405	[»]
2VGT	X-ray	1.86	A	1-405	[»]
2VGU	X-ray	1.80	A	1-405	[»]
2VGV	X-ray	2.30	A	1-405	[»]
2VGW	X-ray	1.86	A	1-405	[»]
2VI8	X-ray	1.67	A	1-405	[»]
2VI9	X-ray	2.00	A	1-405	[»]
2VIA	X-ray	1.67	A	1-405	[»]
2VIB	X-ray	1.85	A	1-405	[»]
2VMN	X-ray	1.74	A	1-405	[»]
2VMO	X-ray	1.74	A	1-405	[»]
2VMP	X-ray	1.74	A	1-405	[»]
2VMQ	X-ray	1.67	A	1-405	[»]
2VMR	X-ray	1.70	A	1-405	[»]
2VMS	X-ray	2.15	A	1-405	[»]
2VMT	X-ray	1.72	A	1-405	[»]
2VMU	X-ray	1.84	A	1-405	[»]
2VMV	X-ray	1.70	A	1-405	[»]
2VMW	X-ray	1.73	A	1-405	[»]
2VMX	X-ray	1.82	A	1-405	[»]
2VMY	X-ray	2.70	A/B	1-405	[»]
2VMZ	X-ray	1.70	A	1-405	[»]
2W7D	X-ray	1.80	A	1-405	[»]
2W7E	X-ray	1.69	A	1-405	[»]
2W7F	X-ray	1.67	A	1-405	[»]
2W7G	X-ray	1.92	A	1-405	[»]
2W7H	X-ray	1.67	A	1-405	[»]
2W7I	X-ray	2.72	A	1-405	[»]
2W7J	X-ray	1.68	A	1-405	[»]
2W7K	X-ray	2.42	A	1-405	[»]
2W7L	X-ray	2.41	A	1-405	[»]
2W7M	X-ray	1.86	A	1-405	[»]

ProteinModelPortal

Q7SIB6.

SMR

Q7SIB6. Positions 1-405.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_00051. SHMT.
[Tree]

InterPro

IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.

PANTHER

PTHR11680. Gly_HO-Metrfase. 1 hit.

Pfam

PF00464. SHMT. 1 hit.
[Graphical view]

PIRSF

PIRSF000412. SHMT. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00096. SHMT. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

Q7SIB6_GEOSE

Accession

Primary (citable) accession number: Q7SIB6

Entry history

Integrated into UniProtKB/TrEMBL:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	December 14, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)