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Database: UniProt
Entry: A0A0M8XQE3_9ACTN
LinkDB: A0A0M8XQE3_9ACTN
Original site: A0A0M8XQE3_9ACTN 
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
//
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