Reviewed, UniProtKB/Swiss-Prot P71753 (SIR_MYCTU)

Names and origin

Protein names

Recommended name:
    Sulfite reductase [ferredoxin]
    EC=1.8.7.1

Gene names

Name:	sir
Synonyms:	nirA
Ordered Locus Names:	Rv2391, MT2461

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	555 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrogen sulfide + 6 oxidized ferredoxin + 3 H2O = sulfite + 6 reduced ferredoxin + 6 H+. Ref.3
Cofactor	Binds 1 siroheme per subunit. Ref.3 Binds 1 4Fe-4S cluster per subunit. Ref.3
Subunit structure	Monomer. Ref.3
Sequence similarities	Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Ontologies

Keywords
Ligand	4Fe-4S Heme Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
PTM	Thioether bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro sulfite reductase (ferredoxin) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 555

555

Sulfite reductase [ferredoxin]

PRO_0000199952

Sites

Metal binding

417

1

Iron-sulfur (4Fe-4S)

Metal binding

423

1

Iron-sulfur (4Fe-4S)

Metal binding

463

1

Iron-sulfur (4Fe-4S)

Metal binding

467

1

Iron (siroheme axial ligand)

Metal binding

467

1

Iron-sulfur (4Fe-4S)

Amino acid modifications

Cross-link

69 ↔ 161

3'-(S-cysteinyl)-tyrosine (Tyr-Cys)

Experimental info

Mutagenesis

69

1

Y → A or F: Strong decrease in activity. Ref.3

Mutagenesis

161

1

C → A or S: Strong decrease in activity. Ref.3

Secondary structure

1

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555

Helix Strand Turn

Details...

Helix

15 – 17

3

Helix

25 – 29

5

Helix

30 – 32

3

Helix

35 – 37

3

Helix

38 – 44

7

Helix

46 – 49

4

Helix

51 – 53

3

Helix

56 – 60

5

Helix

62 – 66

5

Beta strand

68 – 72

5

Helix

78 – 80

3

Helix

83 – 85

3

Helix

86 – 89

4

Beta strand

90 – 99

10

Helix

101 – 103

3

Helix

107 – 120

14

Beta strand

124 – 127

4

Beta strand

133 – 138

6

Helix

140 – 142

3

Helix

143 – 151

9

Turn

152 – 154

3

Beta strand

160 – 170

11

Turn

172 – 176

5

Helix

185 – 195

11

Helix

199 – 201

3

Beta strand

208 – 216

9

Helix

220 – 222

3

Beta strand

223 – 232

10

Turn

233 – 235

3

Beta strand

236 – 243

8

Beta strand

248 – 250

3

Beta strand

255 – 261

7

Helix

263 – 265

3

Helix

266 – 280

15

Helix

286 – 288

3

Helix

291 – 298

8

Helix

300 – 310

11

Beta strand

333 – 337

5

Beta strand

340 – 347

8

Beta strand

352 – 354

3

Helix

355 – 368

14

Beta strand

373 – 375

3

Beta strand

381 – 386

6

Helix

388 – 400

13

Beta strand

404 – 406

3

Helix

409 – 413

5

Beta strand

414 – 416

3

Helix

419 – 421

3

Helix

431 – 444

14

Helix

446 – 449

4

Beta strand

458 – 463

6

Helix

470 – 472

3

Beta strand

473 – 487

15

Beta strand

489 – 498

10

Turn

518 – 520

3

Helix

521 – 534

14

Helix

542 – 548

7

Helix

551 – 554

4

Sequences

	Sequence		Length	Mass (Da)
	P71753-1 [UniParc]. Last modified September 27, 2005. Version 2. Checksum: 68925CA37C131BC3	FASTA	555	62,112
	10 20 30 40 50 60 MTTARPAKAR NEGQWALGHR EPLNANEELK KAGNPLDVRE RIENIYAKQG FDSIDKTDLR 70 80 90 100 110 120 GRFRWWGLYT QREQGYDGTW TGDDNIDKLE AKYFMMRVRC DGGALSAAAL RTLGQISTEF 130 140 150 160 170 180 ARDTADISDR QNVQYHWIEV ENVPEIWRRL DDVGLQTTEA CGDCPRVVLG SPLAGESLDE 190 200 210 220 230 240 VLDPTWAIEE IVRRYIGKPD FADLPRKYKT AISGLQDVAH EINDVAFIGV NHPEHGPGLD 250 260 270 280 290 300 LWVGGGLSTN PMLAQRVGAW VPLGEVPEVW AAVTSVFRDY GYRRLRAKAR LKFLIKDWGI 310 320 330 340 350 360 AKFREVLETE YLKRPLIDGP APEPVKHPID HVGVQRLKNG LNAVGVAPIA GRVSGTILTA 370 380 390 400 410 420 VADLMARAGS DRIRFTPYQK LVILDIPDAL LDDLIAGLDA LGLQSRPSHW RRNLMACSGI 430 440 450 460 470 480 EFCKLSFAET RVRAQHLVPE LERRLEDINS QLDVPITVNI NGCPNSCARI QIADIGFKGQ 490 500 510 520 530 540 MIDDGHGGSV EGFQVHLGGH LGLDAGFGRK LRQHKVTSDE LGDYIDRVVR NFVKHRSEGE 550 RFAQWVIRAE EDDLR

References

	« Hide 'large scale' referencesShow 'large scale' 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.
[3]	"Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site." Schnell R., Sandalova T., Hellman U., Lindqvist Y., Schneider G. J. Biol. Chem. 280:27319-27328(2005) [PubMed: 15917234] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-69 AND CYS-161. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBLGenBankDDBJ

BX842579 Genomic DNA. Translation: CAB03734.1. Different initiation.
AE000516 Genomic DNA. Translation: AAK46756.1.

PIR

B70682.

RefSeq

NP_216907.1.
NP_336942.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZJ8	X-ray	2.80	A/B	3-555	[»]
1ZJ9	X-ray	2.90	A/B	3-555	[»]

ModBase

Search...

Genome annotation databases

GeneID

885472.
925885.

GenomeReviews

Gene locus MT2461 in contig AE000516_GR.
Gene locus Rv2391 in contig AL123456_GR.

KEGG

mtc:MT2461.
mtu:Rv2391.

TIGR

MT2461.

Organism-specific databases

TubercuList

Rv2391.

Phylogenomic databases

HOGENOM

P71753.

OMA

P71753. HINISGC.

Enzyme and pathway databases

BRENDA

1.8.7.1. 809.

Family and domain databases

InterPro

IPR006066. Nir_Si_BS.
IPR006067. Nir_Sir_4Fe4S.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
[Graphical view]

Pfam

PF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]

PRINTS

PR00397. SIROHAEM.

PROSITE

PS00365. NIR_SIR. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SIR_MYCTU

Accession

Primary (citable) accession number: P71753
Secondary accession number(s): Q7D781

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	September 27, 2005
Last modified:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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