Reviewed, UniProtKB/Swiss-Prot Q10600 (CYSNC_MYCTU)

Names and origin

Protein names

Recommended name:
    Bifunctional enzyme cysN/cysC
Including the following 2 domains:
    1- Recommended name:
            Sulfate adenylyltransferase subunit 1
              EC=2.7.7.4
        Alternative name(s):
            Sulfate adenylate transferase
              Short name=SAT
            ATP-sulfurylase large subunit
    2- Recommended name:
            Adenylyl-sulfate kinase
              EC=2.7.1.25
        Alternative name(s):
            APS kinase
            ATP adenosine-5'-phosphosulfate 3'-phosphotransferase

Gene names

Name:	cysNC
Synonyms:	cysN
Ordered Locus Names:	Rv1286, MT1324
ORF Names:	MTCY373.05

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	614 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity By similarity. APS kinase catalyzes the synthesis of activated sulfate By similarity.
Catalytic activity	ATP + sulfate = diphosphate + adenylyl sulfate. HAMAP MF_00062 ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate. HAMAP MF_00062
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. HAMAP MF_00062 Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Subunit structure	Heterodimer composed of cysD, the smaller subunit, and cysN By similarity.
Sequence similarities	In the N-terminal section; belongs to the GTP-binding elongation factor family. CysN/nodQ subfamily. In the C-terminal section; belongs to the APS kinase family.

Ontologies

Keywords
Ligand	ATP-binding GTP-binding Nucleotide-binding
Molecular function	Kinase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	sulfate assimilation Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: InterPro adenylylsulfate kinase activity Inferred from electronic annotation. Source: HAMAP 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 – 614	614	Bifunctional enzyme cysN/cysC HAMAP MF_00062		PRO_0000091537
Regions
	Nucleotide binding	11 – 18	8	GTP By similarity
	Nucleotide binding	88 – 92	5	GTP By similarity
	Nucleotide binding	143 – 146	4	GTP By similarity
	Nucleotide binding	450 – 457	8	ATP Potential
	Region	1 – 441	441	Sulfate adenylyltransferase HAMAP MF_00062
	Region	442 – 614	173	Adenylyl-sulfate kinase HAMAP MF_00062
Sites
	Active site	524	1	Phosphoserine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10600-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 2C3709C8B91867C4	FASTA	614	67,839
	10 20 30 40 50 60 MTTLLRLATA GSVDDGKSTL IGRLLYDSKA VMEDQWASVE QTSKDRGHDY TDLALVTDGL 70 80 90 100 110 120 RAEREQGITI DVAYRYFATP KRKFIIADTP GHIQYTRNMV TGASTAQLVI VLVDARHGLL 130 140 150 160 170 180 EQSRRHAFLA SLLGIRHLVL AVNKMDLLGW DQEKFDAIRD EFHAFAARLD VQDVTSIPIS 190 200 210 220 230 240 ALHGDNVVTK SDQTPWYEGP SLLSHLEDVY IAGDRNMVDV RFPVQYVIRP HTLEHQDHRS 250 260 270 280 290 300 YAGTVASGVM RSGDEVVVLP IGKTTRITAI DGPNGPVAEA FPPMAVSVRL ADDIDISRGD 310 320 330 340 350 360 MIARTHNQPR ITQEFDATVC WMADNAVLEP GRDYVVKHTT RTVRARIAGL DYRLDVNTLH 370 380 390 400 410 420 RDKTATALKL NELGRVSLRT QVPLLLDEYT RNASTGSFIL IDPDTNGTVA AGMVLRDVSA 430 440 450 460 470 480 RTPSPNTVRH RSLVTAQDRP PRGKTVWFTG LSGSGKSSVA MLVERKLLEK GISAYVLDGD 490 500 510 520 530 540 NLRHGLNADL GFSMADRAEN LRRLSHVATL LADCGHLVLV PAISPLAEHR ALARKVHADA 550 560 570 580 590 600 GIDFFEVFCD TPLQDCERRD PKGLYAKARA GEITHFTGID SPYQRPKNPD LRLTPDRSID 610 EQAQEVIDLL ESSS

References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX842576 Genomic DNA. Translation: CAA97752.1. AE000516 Genomic DNA. Translation: AAK45585.1.
PIR	B70772.
RefSeq	NP_215802.1. NP_335771.1.
3D structure databases
HSSP	HSSP built from PDB template 1M7G based on UniProtKB Q12657.
ModBase	Search...
Genome annotation databases
GeneID	886978. 924747.
GenomeReviews	Gene locus MT1324 in contig AE000516_GR. Gene locus Rv1286 in contig AL123456_GR.
KEGG	mtc:MT1324. mtu:Rv1286.
TIGR	MT1324.
Organism-specific databases
TubercuList	Rv1286.
Phylogenomic databases
HOGENOM	Q10600.
OMA	Q10600. IILVDAT.
Enzyme and pathway databases
BRENDA	2.7.1.25. 809. 2.7.7.4. 809.
Family and domain databases
HAMAP	MF_00062. Fused. [Tree] MF_00065. Fused. [Tree]
InterPro	IPR002891. APS_kinase_C. IPR000795. ProtSyn_GTP_bd. IPR011779. SO4_adenylTrfase_lsu. IPR004161. Transl_elong_EFTu/EF1A_2. [Graphical view]
Pfam	PF01583. APS_kinase. 1 hit. PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
ProDom	PD002350. APS_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00455. apsK. 1 hit. TIGR02034. CysN. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSNC_MYCTU

Accession

Primary (citable) accession number: Q10600

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 73 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)