Reviewed, UniProtKB/Swiss-Prot A0L6E2 (CYSD_MAGSM)

Names and origin

Protein names

Recommended name:
    Sulfate adenylyltransferase subunit 2
    EC=2.7.7.4
Alternative name(s):
    Sulfate adenylate transferase
      Short name=SAT
    ATP-sulfurylase small subunit

Gene names

Name:	cysD
Ordered Locus Names:	Mmc1_1017

Organism

Magnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP]

Taxonomic identifier

156889 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Magnetococcus

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + sulfate = diphosphate + adenylyl sulfate. HAMAP MF_00064
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. HAMAP MF_00064
Subunit structure	Heterodimer composed of cysD, the smaller subunit, and cysN By similarity.
Sequence similarities	Belongs to the PAPS reductase family. CysD subfamily.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	sulfate assimilation Inferred from electronic annotation. Source: HAMAP sulfate reduction Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW sulfate adenylyltransferase (ATP) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 300	300	Sulfate adenylyltransferase subunit 2 HAMAP MF_00064		PRO_0000340198

Sequences

	Sequence		Length	Mass (Da)
	A0L6E2-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 31EE671A58CA59E2	FASTA	300	34,325
	10 20 30 40 50 60 MTMKTHLQRL EAESIHIMRE VVAQFRKPVM LYSIGKDSSV MLHLALKAFY PGKPPFPLLH 70 80 90 100 110 120 VDTTWKFREM IVFRDQRVKA LGLDLRVHIN QEGIAQGITP FNQSASIYTD IMKTQSLKQA 130 140 150 160 170 180 LEQGGFDAAF GGARRDEEKS RAKERIFSFR TPNHRWDPKN QRPELWNLYN GRIAPGESIR 190 200 210 220 230 240 VFPLSNWTEL DIWQYIHQEQ IPVVPLYFAQ PRPVVVRHGA LIMVDDGRMP LLPGEEPSLR 250 260 270 280 290 300 SVRFRTLGCY PLTGAVESTT TDVAGIIGEM LVAHRSEREG RVIDHDGGAS MEEKKQEGYF

References

[1]

"Complete sequence of Magnetococcus sp. MC-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000471 Genomic DNA. Translation: ABK43535.1.
RefSeq	YP_864941.1.
3D structure databases
SMR	A0L6E2. Positions 5-209.
ModBase	Search...
Protein-protein interaction databases
STRING	A0L6E2.
Genome annotation databases
GeneID	4482338.
GenomeReviews	Gene locus Mmc1_1017 in contig CP000471_GR.
KEGG	mgm:Mmc1_1017.
NMPDR	fig|156889.1.peg.2645.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	SLRVFPL.
Family and domain databases
HAMAP	MF_00064. [Tree]
InterPro	IPR002500. PAPS_reduct. IPR014729. Rossmann-like_a/b/a_fold. IPR011784. SO4_adenylTrfase_ssu. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
Pfam	PF01507. PAPS_reduct. 1 hit. [Graphical view]
PIRSF	PIRSF002936. CysDAde_trans. 1 hit.
TIGRFAMs	TIGR02039. CysD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CYSD_MAGSM

Accession

Primary (citable) accession number: A0L6E2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	December 12, 2006
Last modified:	November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)