CAN_HAEIN
ID CAN_HAEIN Reviewed; 229 AA.
AC P45148;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Carbonic anhydrase 2;
DE EC=4.2.1.1 {ECO:0000269|PubMed:16584170};
DE AltName: Full=Carbonate dehydratase 2;
GN Name=can; OrderedLocusNames=HI_1301;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ZINC ION, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RX PubMed=16584170; DOI=10.1021/bi052272q;
RA Cronk J.D., Rowlett R.S., Zhang K.Y., Tu C., Endrizzi J.A., Lee J.,
RA Gareiss P.C., Preiss J.R.;
RT "Identification of a novel noncatalytic bicarbonate binding site in
RT eubacterial beta-carbonic anhydrase.";
RL Biochemistry 45:4351-4361(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC Evidence={ECO:0000269|PubMed:16584170};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16584170};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16584170};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22946.1; -; Genomic_DNA.
DR PIR; F64170; F64170.
DR RefSeq; NP_439452.1; NC_000907.1.
DR RefSeq; WP_005631770.1; NC_000907.1.
DR PDB; 2A8C; X-ray; 2.30 A; A/B/C/D/E/F=1-229.
DR PDB; 2A8D; X-ray; 2.20 A; A/B/C/D/E/F=1-229.
DR PDB; 3E1V; X-ray; 2.80 A; A/B=1-229.
DR PDB; 3E1W; X-ray; 2.60 A; A/B=1-229.
DR PDB; 3E24; X-ray; 2.30 A; A/B=1-229.
DR PDB; 3E28; X-ray; 2.50 A; A/B/C/D/E/F=1-229.
DR PDB; 3E2A; X-ray; 2.30 A; A/B/C/D/E/F=1-229.
DR PDB; 3E2W; X-ray; 2.30 A; A/B/C/D/E/F=1-229.
DR PDB; 3E2X; X-ray; 2.55 A; A/B=1-229.
DR PDB; 3E31; X-ray; 2.95 A; A/B=1-229.
DR PDB; 3E3F; X-ray; 2.30 A; A/B=1-229.
DR PDB; 3E3G; X-ray; 2.30 A; A/B/C/D/E/F=1-229.
DR PDB; 3E3I; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-229.
DR PDB; 3MF3; X-ray; 2.50 A; A/B/C/D/E/F=1-221.
DR PDB; 4WAJ; X-ray; 2.70 A; A/B=1-229.
DR PDB; 4WAK; X-ray; 2.49 A; A/B=1-229.
DR PDB; 4WAM; X-ray; 2.20 A; A/B=1-229.
DR PDBsum; 2A8C; -.
DR PDBsum; 2A8D; -.
DR PDBsum; 3E1V; -.
DR PDBsum; 3E1W; -.
DR PDBsum; 3E24; -.
DR PDBsum; 3E28; -.
DR PDBsum; 3E2A; -.
DR PDBsum; 3E2W; -.
DR PDBsum; 3E2X; -.
DR PDBsum; 3E31; -.
DR PDBsum; 3E3F; -.
DR PDBsum; 3E3G; -.
DR PDBsum; 3E3I; -.
DR PDBsum; 3MF3; -.
DR PDBsum; 4WAJ; -.
DR PDBsum; 4WAK; -.
DR PDBsum; 4WAM; -.
DR AlphaFoldDB; P45148; -.
DR SMR; P45148; -.
DR STRING; 71421.HI_1301; -.
DR EnsemblBacteria; AAC22946; AAC22946; HI_1301.
DR KEGG; hin:HI_1301; -.
DR PATRIC; fig|71421.8.peg.1353; -.
DR eggNOG; COG0288; Bacteria.
DR HOGENOM; CLU_053879_3_0_6; -.
DR OMA; PANEIIG; -.
DR PhylomeDB; P45148; -.
DR BioCyc; HINF71421:G1GJ1-1326-MON; -.
DR BRENDA; 4.2.1.1; 2529.
DR EvolutionaryTrace; P45148; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0015976; P:carbon utilization; IDA:UniProtKB.
DR Gene3D; 3.40.1050.10; -; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; PTHR11002; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; SSF53056; 1.
DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..229
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000077467"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16584170,
FT ECO:0007744|PDB:2A8C, ECO:0007744|PDB:2A8D"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16584170,
FT ECO:0007744|PDB:2A8C, ECO:0007744|PDB:2A8D"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16584170,
FT ECO:0007744|PDB:2A8C, ECO:0007744|PDB:2A8D"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16584170,
FT ECO:0007744|PDB:2A8C, ECO:0007744|PDB:2A8D"
FT HELIX 2..20
FT /evidence="ECO:0007829|PDB:3E3I"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:4WAJ"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:2A8D"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:3E3I"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:3E31"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:3E3I"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3E2X"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:3E3I"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:3E3I"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:3E3I"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3E3I"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:3E3I"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2A8D"
SQ SEQUENCE 229 AA; 26250 MW; 4EB20478BC9EB6C9 CRC64;
MDKIKQLFAN NYSWAQRMKE ENSTYFKELA DHQTPHYLWI GCSDSRVPAE KLTNLEPGEL
FVHRNVANQV IHTDFNCLSV VQYAVDVLKI EHIIICGHTN CGGIHAAMAD KDLGLINNWL
LHIRDIWFKH GHLLGKLSPE KRADMLTKIN VAEQVYNLGR TSIVKSAWER GQKLSLHGWV
YDVNDGFLVD QGVMATSRET LEISYRNAIA RLSILDEENI LKKDHLENT
