Q4P829 (Q4P829_USTMA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase RuleBase RU000548
EC=3.3.1.1 RuleBase RU000548

Gene names

ORF Names:

UM03734.1 EMBL EAK84912.1

Organism

Ustilago maydis (strain 521 / FGSC 9021) (Smut fungus)

Taxonomic identifier

237631 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. RuleBase RU000548
Cofactor	NAD By similarity. RuleBase RU000548
Pathway	Amino-acid biosynthesis; homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. RuleBase RU000548
Sequence similarities	Belongs to the adenosylhomocysteinase family. RuleBase RU004166

Ontologies

Keywords
Biological process	One-carbon metabolism RuleBase RU000548
Ligand	NAD RuleBase RU000548
Molecular function	Hydrolase RuleBase RU000548
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	adenosylhomocysteinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Binding site	54	1	Substrate By similarity PIRSR PIRSR001109-1
	Binding site	128	1	Substrate By similarity PIRSR PIRSR001109-1
	Binding site	153	1	Substrate By similarity PIRSR PIRSR001109-1
	Binding site	183	1	Substrate By similarity PIRSR PIRSR001109-1
	Binding site	187	1	Substrate By similarity PIRSR PIRSR001109-1

Sequences

	Sequence		Length	Mass (Da)
	Q4P829 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 47324F712E9F7281	FASTA	431	47,035
	10 20 30 40 50 60 MPNYKVADIS LAAFGRKEIE IAEGEMPGLM ALRTKYGAEQ PLKGARIAGS LHMTIQTAVL 70 80 90 100 110 120 IETLVALGAQ VTWASCNIFS TQDHAAAAIA ATGVPVFAWK GETEEEYDWC LEQTLTAHPE 130 140 150 160 170 180 GPNMILDDGG DLTWLVHDKH PQLLEQIKGV SEETTTGVHI LYSAMKKGTL KLPAINVNDS 190 200 210 220 230 240 VTKSKFDNYY GCRESLVDGI KRATDVMLGG KVAIVAGFGD VGKGCAESLR GYGCRVIVTE 250 260 270 280 290 300 IDPINALQAS MAGYQVDIMD DVASQADIFV TTTGCRDIIT GKHFEAMKDD AIVCNIGHFD 310 320 330 340 350 360 IEIDVAWLKA NAQSVSNIKP QVDRYTLKNG NRIILLAEGR LVNLGCATGH PSFIMSASFC 370 380 390 400 410 420 NQTLAQIALW NDKAGQYKRG EVYMLPKELD EEVALAHLGR LNVKLTKLTK VQADYLDLPV 430 DGPYKRDTYR Y

References

[1]

"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521 / FGSC 9021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACP01000124 Genomic DNA. Translation: EAK84912.1.
RefSeq	XP_759881.1. XM_754788.1.
3D structure databases
ProteinModelPortal	Q4P829.
SMR	Q4P829. Positions 4-431.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4P829.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	UM03734T0; UM03734P0; UM03734.
GeneID	3631783.
KEGG	uma:UM03734.1.
Phylogenomic databases
eggNOG	fuNOG06806.
HOGENOM	HBG352029.
OMA	ELFTKTE.
OrthoDB	EOG41G6CK.
Family and domain databases
HAMAP	MF_00563. AdoHcyase. [Tree]
InterPro	IPR000043. Adenosylhomocysteinase. IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view]
KO	K01251.
PANTHER	PTHR23420. Ad_hcy_hydrolase. 1 hit.
Pfam	PF05221. AdoHcyase. 1 hit. PF00670. AdoHcyase_NAD. 1 hit. [Graphical view]
PIRSF	PIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMART	SM00996. AdoHcyase. 1 hit. SM00997. AdoHcyase_NAD. 1 hit. [Graphical view]
TIGRFAMs	TIGR00936. AhcY. 1 hit.
PROSITE	PS00738. ADOHCYASE_1. 1 hit. PS00739. ADOHCYASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q4P829_USTMA

Accession

Primary (citable) accession number: Q4P829

Entry history

Integrated into UniProtKB/TrEMBL:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)