ID J9SHZ0_9ACTN Unreviewed; 761 AA.
AC J9SHZ0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN ORFNames=KTR9_4506 {ECO:0000313|EMBL:AFR51110.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR51110.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR51110.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR51110.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
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; CP002907; AFR51110.1; -; Genomic_DNA.
DR AlphaFoldDB; J9SHZ0; -.
DR STRING; 337191.KTR9_4506; -.
DR KEGG; gor:KTR9_4506; -.
DR PATRIC; fig|337191.3.peg.4917; -.
DR eggNOG; COG0288; Bacteria.
DR eggNOG; COG0659; Bacteria.
DR HOGENOM; CLU_003182_11_0_11; -.
DR Proteomes; UP000003281; Chromosome.
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 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 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 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 16..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..368
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
FT REGION 491..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 79300 MW; 762B4B4EF6EED575 CRC64;
MGSRGPGIRE VVRYDLPASL VVFLVALPLS LGIAIASDAP VLAGLIAAVV GGIVAGLIGG
SALQVSGPAA GLTVVVADMV ANFGWRVTCF ITVGAGVLQI LFGLSRIAGA ALAIAPVVVH
AMLAGIGITI ALQQIHVLLG GSSASSAWEN VTSLPAGLAD IETSDALVGG TVIAVLLIWP
LMPAAVRKVP GPLVAIVGAT ALTIVFGLDV ERISIDGNFF EAITLPELPD SSWAAVLLGV
LTVALIASVE SLLSAVAVDK MHTGPRSDLN RELLGQGSAN ITSGMLGGLP VTGVIVRSTT
NVNSGARTSA SAVMHGVWVL VFAALLTGLV EQIPMAALAG LLVVIGIQLV KLAHMRIALR
TGDLWVYVIT VVAVVFLNLL EGVGIGLAVA IGLVVWRVVR AEIISEASGT DDGAQQWTVR
VRGSLSFLSL PKLNKALSQV PDGAHLTLEL DTDFLDNAAS EMLEDFRWAH EAGGGTVLVV
EKGRARLVDA PRRPPRRHTS GFAGLTPWRN RTESETSVDS DRPAALRSVL GGVDEYENEH
ADALRAMLAD VTEAQDPDSF FVTCADSRLL PNIITASGPG DLFTVRNVGN LIPTDSDDVS
VEAALEFAIG ELGVSSIVVC GHSSCGAMHA LLDSERSADH DHQTGSATPS EQTPIQRWLK
HAVPSRVAFR HGHPAGRAAA ELGMAEVDQL AVVNVAKQIE TLARHPLVGR AAADARLRIV
GLYFDIATAR VYEVTPQSIA PVTGDDSLRS RRRDPETTSA R
//
