ID C1BD38_RHOOB Unreviewed; 581 AA.
AC C1BD38;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN OrderedLocusNames=ROP_pROB01-02830 {ECO:0000313|EMBL:BAH55782.1};
OS Rhodococcus opacus (strain B4).
OG Plasmid pROB01 {ECO:0000313|EMBL:BAH55782.1,
OG ECO:0000313|Proteomes:UP000002212}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH55782.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH55782.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH55782.1,
RC ECO:0000313|Proteomes:UP000002212};
RC PLASMID=pROB01 {ECO:0000313|EMBL:BAH55782.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217}.
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DR EMBL; AP011116; BAH55782.1; -; Genomic_DNA.
DR AlphaFoldDB; C1BD38; -.
DR KEGG; rop:ROP_pROB01-02830; -.
DR PATRIC; fig|632772.20.peg.8017; -.
DR HOGENOM; CLU_003182_11_0_11; -.
DR OrthoDB; 9771198at2; -.
DR Proteomes; UP000002212; Plasmid pROB01.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR011547; SLC26A/SulP_dom.
DR PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11002:SF83; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR Pfam; PF00916; Sulfate_transp; 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:BAH55782.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Plasmid {ECO:0000313|EMBL:BAH55782.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 54..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..181
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 61089 MW; 207BBF978FC5A1DA CRC64;
MPPTTTTQSD DPPTAADDSA KPAPWLPRVL RHDLPASLVV FLVALPALPD GQWLGVATGV
LTVALIASVE SLLSAVSVDK MHTGPRADLN RELLGQGAAN ITSGVLGGLP VTGVIVRSAT
NVNAGARTRA SATLHGVWVL VFSALLAGLV QQIPNSVLAG LLIVIGIQLI KLAHLRIAHR
TGDLWVYGVT AAAVVFLNLL EGVLIGLALA VALVVWRVVR ASIHAEPVGT PQSRQWRVVV
EGSCSFLALP RLTSVLASVP PDSHVTIELT VDFLDHAAYE VIEEWSRQHE SNGGTVLIDE
RGTAEMAAAA AGPPTRTTDG TAQLSRRGGF APWRVWQKFH LHHTPDGQTK QPGPRALRSV
LAGISDYHRT HAPHLRPHMD DLHDGQNPDA LFLTCSDSRI VPNIITSSGP GDLFTVRNIG
NLVPAGERDD SVEAALAFAL DELGVSSVLV CGHSGCGAMK ALLADQDQPH PRSGDGLAVG
RWLEHAQPSK RAYLAGHPVA RAAAESGFGA LDQLAMVNVA LQLQTLQRHP LIGAAMSEGR
VHIAGLFFDI PTARVLAVST STIDELDPDS AAAASLSAPL G
//
