ID F2R6Y6_STRVP Unreviewed; 214 AA.
AC F2R6Y6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN OrderedLocusNames=SVEN_0391 {ECO:0000313|EMBL:CCA53678.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53678.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA53678.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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}.
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DR EMBL; FR845719; CCA53678.1; -; Genomic_DNA.
DR RefSeq; WP_015031597.1; NZ_JABVZO010000218.1.
DR AlphaFoldDB; F2R6Y6; -.
DR STRING; 953739.SVEN_0391; -.
DR GeneID; 69862605; -.
DR KEGG; sve:SVEN_0391; -.
DR PATRIC; fig|953739.5.peg.5959; -.
DR eggNOG; COG0288; Bacteria.
DR HOGENOM; CLU_053879_4_1_11; -.
DR OrthoDB; 9797527at2; -.
DR Proteomes; UP000006854; Chromosome.
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 CDD; cd03378; beta_CA_cladeC; 1.
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, ECO:0000313|EMBL:CCA53678.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 214 AA; 22298 MW; 1A806DC7E1645985 CRC64;
MTEKILTPTP RDAFDLLMAG NKRFVSGAPE HPNQDAARRT ETAPSQQPFA VLFGCSDSRL
AAEIIFDRGL GDLFVVRTAG HVAGTETLGS IEFGVSVLKA PLVVVLGHDS CGAVAAACSA
LDEGKTPGGF VRDVVERVNT SVLAARAAGR ESAEEILAEH IEHTVDLLLE RSRVLADAVA
EGRLGVVGLS YRLADGSAQL VAARGLDVAV PTAS
//
