ID Q2RTM0_RHORT Unreviewed; 259 AA.
AC Q2RTM0;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:ABC22525.1};
DE EC=4.2.1.1 {ECO:0000313|EMBL:ABC22525.1};
GN OrderedLocusNames=Rru_A1725 {ECO:0000313|EMBL:ABC22525.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22525.1, ECO:0000313|Proteomes:UP000001929};
RN [1] {ECO:0000313|EMBL:ABC22525.1, ECO:0000313|Proteomes:UP000001929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC {ECO:0000313|Proteomes:UP000001929};
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718}.
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DR EMBL; CP000230; ABC22525.1; -; Genomic_DNA.
DR RefSeq; WP_011389415.1; NC_007643.1.
DR RefSeq; YP_426812.1; NC_007643.1.
DR AlphaFoldDB; Q2RTM0; -.
DR STRING; 269796.Rru_A1725; -.
DR EnsemblBacteria; ABC22525; ABC22525; Rru_A1725.
DR KEGG; rru:Rru_A1725; -.
DR PATRIC; fig|269796.9.peg.1802; -.
DR eggNOG; COG3338; Bacteria.
DR HOGENOM; CLU_039326_0_2_5; -.
DR PhylomeDB; Q2RTM0; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF265; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ABC22525.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001929};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..259
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004214643"
FT DOMAIN 35..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 259 AA; 27595 MW; 12C7291F0B1FE2AB CRC64;
MVMQRAFSHA AMAVAFGLVG FSGAPAVAAE TAHPPHWAYE GKGGPVDWGA LSEDYHACAA
GKEQSPVDIR DAIPAKLPAI APAYQAQSAV VVNNGHTLQV NVSPGSSLDF RGQRYELLQY
HFHHPSEHLV NGKAAPLELH LVHKGPTALT VIGVMLVPGA ANPAIEAIWK VAPAKEGGEA
TLGDPGPDLG KLLPESKSYT FYEGSLTTPP CSEVVNWINL KTPVTVSEDQ IARFAALFPM
NARPPQALHR RIILESQDQ
//