O53573 (MTCA2_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 2
Short name=Beta-CA 2
EC=4.2.1.1

Alternative name(s):
Carbonate dehydratase 2
mtCA 2

Gene names

Name:	mtcA2
Synonyms:	canB, cynT
Ordered Locus Names:	Rv3588c, MT3694

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible hydration of carbon dioxide to form bicarbonate. Ref.5
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Binds 1 zinc ion per subunit. Ref.5 Ref.6
Enzyme regulation	Inhibited by sulfonamides and sulfamates. Ref.4
Subunit structure	Homotetramer at pH 8.4 and homodimer at pH 7.4. Ref.5 Ref.6
Sequence similarities	Belongs to the beta-class carbonic anhydrase family.
Biophysicochemical properties	pH dependence: Active at pH 8.4 and inactive at pH 7.5. Ref.6

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbon utilization Inferred from electronic annotation. Source: InterPro protein homotetramerization Inferred from physical interaction Ref.6. Source: MTBBASE
Molecular_function	carbonate dehydratase activity Inferred from direct assay Ref.5. Source: MTBBASE zinc ion binding Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 207

207

Carbonic anhydrase 2

PRO_0000396117

Sites

Metal binding

51

1

Zinc

Metal binding

53

1

Zinc

Metal binding

104

1

Zinc

Metal binding

107

1

Zinc

Secondary structure

1

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207

Helix Strand Turn

Details...

Helix

6 – 22

17

Helix

28 – 30

3

Helix

32 – 36

5

Turn

37 – 40

4

Beta strand

45 – 51

7

Helix

58 – 61

4

Beta strand

68 – 74

7

Helix

75 – 77

3

Helix

81 – 92

12

Beta strand

98 – 106

9

Helix

108 – 119

12

Helix

127 – 143

17

Helix

149 – 167

19

Helix

169 – 176

8

Beta strand

181 – 187

7

Turn

189 – 191

3

Beta strand

195 – 201

7

Sequences

	Sequence		Length	Mass (Da)
	O53573 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 60BE85FA14847FEC	FASTA	207	21,792
	10 20 30 40 50 60 MPNTNPVAAW KALKEGNERF VAGRPQHPSQ SVDHRAGLAA GQKPTAVIFG CADSRVAAEI 70 80 90 100 110 120 IFDQGLGDMF VVRTAGHVID SAVLGSIEYA VTVLNVPLIV VLGHDSCGAV NAALAAINDG 130 140 150 160 170 180 TLPGGYVRDV VERVAPSVLL GRRDGLSRVD EFEQRHVHET VAILMARSSA ISERIAGGSL 190 200 AIVGVTYQLD DGRAVLRDHI GNIGEEV

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Molecular cloning, characterization, and inhibition studies of the Rv1284 beta-carbonic anhydrase from Mycobacterium tuberculosis with sulfonamides and a sulfamate." Minakuchi T., Nishimori I., Vullo D., Scozzafava A., Supuran C.T. J. Med. Chem. 52:2226-2232(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[4]	"Discovery of low nanomolar and subnanomolar inhibitors of the mycobacterial beta-carbonic anhydrases Rv1284 and Rv3273." Guzel O., Maresca A., Scozzafava A., Salman A., Balaban A.T., Supuran C.T. J. Med. Chem. 52:4063-4067(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[5]	"Structure and function of carbonic anhydrases from Mycobacterium tuberculosis." Suarez Covarrubias A., Larsson A.M., Hogbom M., Lindberg J., Bergfors T., Bjorkelid C., Mowbray S.L., Unge T., Jones T.A. J. Biol. Chem. 280:18782-18789(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH COFACTOR, FUNCTION AS AN CARBONIC ANHYDRASE, SUBUNIT, COFACTOR.
[6]	"Structural mechanics of the pH-dependent activity of beta-carbonic anhydrase from Mycobacterium tuberculosis." Covarrubias A.S., Bergfors T., Jones T.A., Hogbom M. J. Biol. Chem. 281:4993-4999(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842583 Genomic DNA. Translation: CAA17857.1.
AE000516 Genomic DNA. Translation: AAK48052.1.
AL123456 Genomic DNA. Translation: CCP46411.1.

PIR

E70804.

RefSeq

NP_218105.1. NC_000962.3.
NP_338238.1. NC_002755.2.
YP_006517078.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YM3	X-ray	1.75	A	2-207	[»]
2A5V	X-ray	2.20	A/B/C/D	2-207	[»]

ProteinModelPortal

O53573.

SMR

O53573. Positions 2-206.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv3588c.

Proteomic databases

PRIDE

O53573.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK48052; AAK48052; MT3694.

GeneID

13317197.
887836.
922804.

KEGG

mtc:MT3694.
mtu:Rv3588c.
mtv:RVBD_3588c.

PATRIC

18129877. VBIMycTub22151_4033.

Organism-specific databases

TubercuList

Rv3588c.

Phylogenomic databases

eggNOG

COG0288.

HOGENOM

HOG000125181.

KO

K01673.

OMA

DSCGAVQ.

ProtClustDB

CLSK792582.

Family and domain databases

Gene3D

3.40.1050.10. 1 hit.

InterPro

IPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]

PANTHER

PTHR11002. PTHR11002. 1 hit.

Pfam

PF00484. Pro_CA. 1 hit.
[Graphical view]

SMART

SM00947. Pro_CA. 1 hit.
[Graphical view]

SUPFAM

SSF53056. Prok_plnt_COanhd. 1 hit.

PROSITE

PS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O53573.

ChEMBL

CHEMBL6068.

EvolutionaryTrace

O53573.

Entry information

Entry name

MTCA2_MYCTU

Accession

Primary (citable) accession number: O53573
Secondary accession number(s): L0TFY5, Q7D582

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 10, 2010
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program