ID A0A0N1GL42_9ACTN Unreviewed; 924 AA.
AC A0A0N1GL42;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:KPI26542.1};
DE EC=4.2.1.1 {ECO:0000313|EMBL:KPI26542.1};
GN ORFNames=OV320_6211 {ECO:0000313|EMBL:KPI26542.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI26542.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI26542.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI26542.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-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 -!- 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:KPI26542.1}.
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DR EMBL; LJCX01000028; KPI26542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1GL42; -.
DR PATRIC; fig|1592329.3.peg.5526; -.
DR Proteomes; UP000037870; 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: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; 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 SUPFAM; SSF52091; SpoIIaa-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KPI26542.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037870};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..406
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 95494 MW; 81CEA966B06A36D3 CRC64;
MSACAPTRTD HSKRTERIHP THSPPPGPHR RFRIAGADVS ASIAVFLIAL PLSLGIALAT
GAPLQAGLVA AAVGGIVAGW VGGAPLQVSG PAAGLTVVTA DLIQRYGWRT TCAITVLAGL
AQLGLGCLRV ARTALAVSPA IVHGMLAGIG VTIAVAQLHV VLGGTPQSSV LDNLRALPAQ
LAGLQPAAVA VSALTLTLLL LWPRIPGRVG SLVQRVPAAL VAVTGATAVA ALAGLTLPKV
DLPSWSSHAL AGLPEGPVLG LMAAVLTTTL VCSVQSLLGA VAVDKLIASR PDLLSARSTR
VGRSDLDREL LGQGAANIVS GALGGLPVAG VAVRSSANVQ AGAVSRNSTM LHGVLVVVAA
LLMVPILDLI PLASLAALVM AVGIQMVSLH HIRTVTRHRE VLVYAVTTLG VVVLGVLEGV
TLGIAVAVAV ALHRLARTRI THHEKEGVHH VHVRGQLTFL AVPRLSRILH LVPQGTHVVV
ELDGSFMDHA AYEALQDWQK THTARGGSVE LTGRRSGTGL DTGTDVEAEA EAETGSETGA
GVDFRSGTGT GIRTGLATST GAGLDTGQGG STAPAAHVRA GEVPIADCRC RPWTPWRNHQ
CEVPRETTQT PQTPQALSPT PTPTPTSLTA QSAESTDAAR PAEATAAGAP ETAQRRGKRE
TPESPESAKP RETKRPPQPG QPEQPGHPGE ERRPGASVEP GEHQLVRGIS AFQRNTAPLV
RGELARLARE GQQPTQLFLT CADSRLVTSM ITSSGPGDLF VVRNVGNLVP PPGEESGDDS
VAAAIEYAVD VLKVRSITVC GHSGCGAMQA LFDTEPGGAR TPLQRWLRHG VPSLERMADG
GRPRARLAGR APVDAVEQLC LTNVVQQLEH LRAHESVTQA LRSGALELHG LYFHVGEAQT
YLLTEAASGD GELFGHVGET GVPA
//
