ID M3BQ31_STRMB Unreviewed; 213 AA.
AC M3BQ31;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN ORFNames=H340_04308 {ECO:0000313|EMBL:EMF01800.1};
OS Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EMF01800.1, ECO:0000313|Proteomes:UP000011740};
RN [1] {ECO:0000313|EMBL:EMF01800.1, ECO:0000313|Proteomes:UP000011740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EMF01800.1,
RC ECO:0000313|Proteomes:UP000011740};
RX PubMed=23558536;
RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT Transglutaminase.";
RL Genome Announc. 1:E0014313-E0014313(2013).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC bicarbonate. {ECO:0000256|ARBA:ARBA00024993}.
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:0000256|ARBA:ARBA00000943};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMF01800.1}.
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DR EMBL; AORZ01000007; EMF01800.1; -; Genomic_DNA.
DR RefSeq; WP_004939886.1; NZ_CP072827.1.
DR AlphaFoldDB; M3BQ31; -.
DR STRING; 1223523.H340_04308; -.
DR PATRIC; fig|1223523.3.peg.875; -.
DR eggNOG; COG0288; Bacteria.
DR Proteomes; UP000011740; Unassembled WGS sequence.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11002:SF13; CARBONIC ANHYDRASE 2; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 213 AA; 21786 MW; 9E5C7B7BEEA9BF19 CRC64;
MTEIQTLTPS GAFALLMAGN GRFVAGRPEH PNQDATRRAE TAPGQQPFAV LFGCSDSRLA
AEIIFDRGLG DLFVVRTAGH VLGPEVLGSI EYGVGILDCP LVVVLGHDSC GAVGAACAAL
EDGVPATGYV RDVVERVTPS VLAARAAGRV EPDEILAEHV KHTADLLLDR SRALAGKVAA
GRAAVVGLSY RLADGSARLV AAHGLDAAAA TAS
//
