GCA1_ARATH
ID GCA1_ARATH Reviewed; 275 AA.
AC Q9FWR5; Q67XH5; Q682H9; Q8LF67; Q9LN36;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Gamma carbonic anhydrase 1, mitochondrial;
DE Short=AtCA1;
DE Short=GAMMA CA1;
DE EC=4.2.1.-;
DE Flags: Precursor;
GN Name=GAMMACA1; OrderedLocusNames=At1g19580; ORFNames=F14P1.8, F18O14.34;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604675; DOI=10.1007/s11103-004-0149-7;
RA Parisi G., Perales M., Fornasari M.S., Colaneri A., Gonzalez-Schain N.,
RA Gomez-Casati D., Zimmermann S., Brennicke A., Araya A., Ferry J.G.,
RA Echave J., Zabaleta E.;
RT "Gamma carbonic anhydrases in plant mitochondria.";
RL Plant Mol. Biol. 55:193-207(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407270; DOI=10.1074/jbc.m511542200;
RA Sunderhaus S., Dudkina N.V., Jaensch L., Klodmann J., Heinemeyer J.,
RA Perales M., Zabaleta E., Boekema E.J., Braun H.-P.;
RT "Carbonic anhydrase subunits form a matrix-exposed domain attached to the
RT membrane arm of mitochondrial complex I in plants.";
RL J. Biol. Chem. 281:6482-6488(2006).
CC -!- FUNCTION: Enzyme involved in the catabolism of H(2)CO(3) but that does
CC not mediates the reversible hydration of carbon dioxide. Mediates
CC complex I assembly in mitochondria and respiration (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotrimer. Component of the mitochondrial oxidoreductase
CC respiratory chain complex I; element of the extra matrix-exposed
CC domain, which is attached to the membrane arm of this complex
CC (Probable). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:15604675}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15604675}; Matrix side
CC {ECO:0000269|PubMed:15604675}. Note=Probably integral to the membrane.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FWR5-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79435.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC024609; AAF98404.1; -; Genomic_DNA.
DR EMBL; AC025808; AAF79435.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29870.1; -; Genomic_DNA.
DR EMBL; AK175388; BAD43151.1; -; mRNA.
DR EMBL; AK176844; BAD44607.1; -; mRNA.
DR EMBL; AK176887; BAD44650.1; -; mRNA.
DR EMBL; AK229264; BAF01128.1; -; mRNA.
DR EMBL; AY085025; AAM61583.1; -; mRNA.
DR PIR; E86328; E86328.
DR RefSeq; NP_564091.1; NM_101815.4. [Q9FWR5-1]
DR PDB; 7A23; EM; 3.70 A; p/q=1-275.
DR PDB; 7A24; EM; 3.80 A; p/q=1-275.
DR PDB; 7AQQ; EM; 3.06 A; z=1-275.
DR PDB; 7AR7; EM; 3.72 A; z=2-234.
DR PDB; 7AR8; EM; 3.53 A; z=1-275.
DR PDB; 7ARB; EM; 3.41 A; z=1-275.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQQ; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9FWR5; -.
DR SMR; Q9FWR5; -.
DR BioGRID; 23784; 27.
DR IntAct; Q9FWR5; 2.
DR STRING; 3702.AT1G19580.1; -.
DR PaxDb; Q9FWR5; -.
DR PRIDE; Q9FWR5; -.
DR ProteomicsDB; 222170; -. [Q9FWR5-1]
DR EnsemblPlants; AT1G19580.1; AT1G19580.1; AT1G19580. [Q9FWR5-1]
DR GeneID; 838545; -.
DR Gramene; AT1G19580.1; AT1G19580.1; AT1G19580. [Q9FWR5-1]
DR KEGG; ath:AT1G19580; -.
DR Araport; AT1G19580; -.
DR TAIR; locus:2013104; AT1G19580.
DR eggNOG; ENOG502QTES; Eukaryota.
DR HOGENOM; CLU_064827_0_0_1; -.
DR InParanoid; Q9FWR5; -.
DR OMA; QEEIAFI; -.
DR PhylomeDB; Q9FWR5; -.
DR BioCyc; ARA:AT1G19580-MON; -.
DR BRENDA; 4.2.1.1; 399.
DR PRO; PR:Q9FWR5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FWR5; baseline and differential.
DR Genevisible; Q9FWR5; AT.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:TAIR.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0045271; C:respiratory chain complex I; IDA:TAIR.
DR GO; GO:0004089; F:carbonate dehydratase activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009853; P:photorespiration; TAS:TAIR.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 2.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lyase; Membrane; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..275
FT /note="Gamma carbonic anhydrase 1, mitochondrial"
FT /id="PRO_0000417610"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 101..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="R -> L (in Ref. 3; BAD44607)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="L -> Q (in Ref. 3; BAD44607)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="E -> D (in Ref. 4; AAM61583)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="K -> R (in Ref. 3; BAD43151)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="V -> L (in Ref. 4; AAM61583)"
FT /evidence="ECO:0000305"
FT HELIX 3..29
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 194..218
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:7AQQ"
SQ SEQUENCE 275 AA; 29971 MW; 7F3D6AF91DB1B8D8 CRC64;
MGTLGRAFYS VGFWIRETGQ ALDRLGCRLQ GKNYFREQLS RHRTLMNVFD KAPIVDKEAF
VAPSASVIGD VHIGRGSSIW YGCVLRGDVN TVSVGSGTNI QDNSLVHVAK SNLSGKVHPT
IIGDNVTIGH SAVLHGCTVE DETFIGMGAT LLDGVVVEKH GMVAAGALVR QNTRIPSGEV
WGGNPARFLR KLTDEEIAFI SQSATNYSNL AQAHAAENAK PLNVIEFEKV LRKKHALKDE
EYDSMLGIVR ETPPELNLPN NILPDKETKR PSNVN
