ID A0A0M8XQE3_9ACTN Unreviewed; 789 AA.
AC A0A0M8XQE3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN ORFNames=ADL05_26510 {ECO:0000313|EMBL:KOX10218.1};
OS Nocardiopsis sp. NRRL B-16309.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX10218.1, ECO:0000313|Proteomes:UP000037694};
RN [1] {ECO:0000313|Proteomes:UP000037694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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}.
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:KOX10218.1}.
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DR EMBL; LGEC01000114; KOX10218.1; -; Genomic_DNA.
DR RefSeq; WP_053619723.1; NZ_LGEC01000114.1.
DR AlphaFoldDB; A0A0M8XQE3; -.
DR STRING; 1519494.ADL05_26510; -.
DR PATRIC; fig|1519494.3.peg.5789; -.
DR OrthoDB; 9771198at2; -.
DR Proteomes; UP000037694; Unassembled WGS sequence.
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 GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR Gene3D; 3.30.750.24; STAS domain; 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 InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814:SF227; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 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.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037694};
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 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..389
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"
FT REGION 761..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 82048 MW; 1AD33BE8C33CB370 CRC64;
MRNDAQGAHP APPPTPAEPT GIHADRKGIA ADVGASFVVF LVAVPMSLGI AVASGAPLMA
GLVAAAVGGI VAGLVGGSMV QVSGPAAGQT IIIADLLLTY GWRVTCLITV LAGLVQLALG
AFRIARAALA VSPAVMHGLL AGVGITIALA QLHVVLGGDP QSSALANLID LPDQIAHNHT
AAVAVGVITI AIMFGWNRLP SLGRLRPSMI PAALVAVGTA TTIAALGGWR VETVSLPDSL
AAAWSLPQLP EAGQWDGIAL AVAAVAMVAS VESLVSAIAI DRRHNGRRVM LNRELMGQGA
ANTVSGALGG LPVAGAIVRS TANVRAGGHS PLSTILHGVW ILLFVALFAH VVELIPMAAL
AALLVFIGVQ MVSVAHLRDL RRHHEASVYL VTMGGVVFLG LLEGVFLGFA LAMVVSLRRL
TKLTVTTEES GDRVHVTVHG SLTFLGVPRL AHVLRTVPAG CRVDLDLHVD FMDHAAFEAI
HAWRVDHERT GGSVDIDEVH EQWYARSSTR SAPAAKTAPG GMARSWAPWD MRGDADREVD
PLALLAAGAR EYHASTADRM RSVMSRLAHG QHPTALFITC ADSRVVPNLI TASGPGDLFT
VRNMGNLVPA PSDTGDGSVG AAIEYAVNVL RVPSIVVCGH SHCGAMQALL DRAHLEQGDA
ATAYMRRWLA TGEASLAHAG AYSGALAGLP TAEALRRLAQ ANVEQQIGHL LDYPLVRERV
ESGALELTGM YYDLESARVH LLDTGTGRFT PVLGVQDVEA PVPHPRADAA GQDQPADESS
SGMSSRSSC
//