NICA_PSEPK
ID NICA_PSEPK Reviewed; 157 AA.
AC Q88FX9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nicotinate dehydrogenase subunit A;
DE EC=1.17.2.1;
DE AltName: Full=Nicotinate degradation protein A;
DE AltName: Full=Nicotinate dehydrogenase small subunit;
GN Name=nicA; Synonyms=ndhS; OrderedLocusNames=PP_3947;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=19118407; DOI=10.1007/s10532-008-9243-x;
RA Yang Y., Yuan S., Chen T., Ma P., Shang G., Dai Y.;
RT "Cloning, heterologous expression, and functional characterization of the
RT nicotinate dehydrogenase gene from Pseudomonas putida KT2440.";
RL Biodegradation 20:541-549(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=18678916; DOI=10.1073/pnas.0802273105;
RA Jimenez J.I., Canales A., Jimenez-Barbero J., Ginalski K., Rychlewski L.,
RA Garcia J.L., Diaz E.;
RT "Deciphering the genetic determinants for aerobic nicotinic acid
RT degradation: the nic cluster from Pseudomonas putida KT2440.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11329-11334(2008).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=21450002; DOI=10.1111/j.1462-2920.2011.02471.x;
RA Jimenez J.I., Juarez J.F., Garcia J.L., Diaz E.;
RT "A finely tuned regulatory circuit of the nicotinic acid degradation
RT pathway in Pseudomonas putida.";
RL Environ. Microbiol. 13:1718-1732(2011).
CC -!- FUNCTION: Subunit of the two-component enzyme NicAB that mediates
CC nicotinate hydroxylation, the first step in the aerobic nicotinate
CC degradation pathway. Mediates conversion of nicotinate into 6-
CC hydroxynicotinate (6HNA). {ECO:0000269|PubMed:18678916,
CC ECO:0000269|PubMed:19118407}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome] + H2O + nicotinate = 6-
CC hydroxynicotinate + 2 Fe(II)-[cytochrome] + 2 H(+);
CC Xref=Rhea:RHEA:27417, Rhea:RHEA-COMP:11777, Rhea:RHEA-COMP:11778,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:32544, ChEBI:CHEBI:57664; EC=1.17.2.1;
CC Evidence={ECO:0000269|PubMed:18678916};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation.
CC {ECO:0000269|PubMed:18678916}.
CC -!- INDUCTION: Repressed by NicS in the absence of 6-hydroxynicotinate
CC (6HNA) or nicotinate inducers. In presence of 6HNA, repression is
CC alleviated. {ECO:0000269|PubMed:21450002}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking both nicA and nicB lack the ability
CC to hydroxylate nicotinate. Cells do not grow in a nicotinate medium but
CC grow in a 6-hydroxynicotinate medium. {ECO:0000269|PubMed:18678916,
CC ECO:0000269|PubMed:19118407}.
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DR EMBL; EU604833; ACC64339.1; -; Genomic_DNA.
DR EMBL; AE015451; AAN69541.1; -; Genomic_DNA.
DR RefSeq; NP_746077.1; NC_002947.4.
DR RefSeq; WP_010954764.1; NC_002947.4.
DR AlphaFoldDB; Q88FX9; -.
DR SMR; Q88FX9; -.
DR STRING; 160488.PP_3947; -.
DR EnsemblBacteria; AAN69541; AAN69541; PP_3947.
DR KEGG; ppu:PP_3947; -.
DR PATRIC; fig|160488.4.peg.4203; -.
DR eggNOG; COG2080; Bacteria.
DR HOGENOM; CLU_052511_3_0_6; -.
DR OMA; RSCVIPL; -.
DR PhylomeDB; Q88FX9; -.
DR BioCyc; MetaCyc:G1G01-4212-MON; -.
DR BioCyc; PPUT160488:G1G01-4212-MON; -.
DR BRENDA; 1.17.2.1; 5092.
DR UniPathway; UPA01010; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016725; F:oxidoreductase activity, acting on CH or CH2 groups; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..157
FT /note="Nicotinate dehydrogenase subunit A"
FT /id="PRO_0000418464"
FT DOMAIN 3..79
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 41
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 157 AA; 16686 MW; 762443DA5987439D CRC64;
MQTTISLQVN GQPVEVSAMP DTPLLLILRN DLCLNGPKYG CGLGECGACT VIIDGVAARS
CVIPLAGAAG RNITTLEGLG SKAAPHPVQQ AFIDEQAAQC GYCMNGMIMT AKALLDRIPE
PSDEQIRNEL SANLCRCGTH VEILRAVRRA AETRRKP
