ID   NIRL_PSEAE              Reviewed;         174 AA.
AC   P95413; Q7DCL3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Siroheme decarboxylase NirL subunit {ECO:0000305};
DE            EC=4.1.1.111 {ECO:0000250|UniProtKB:I6UH61};
GN   Name=nirL {ECO:0000303|PubMed:8982003}; OrderedLocusNames=PA0514;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=8982003; DOI=10.1128/jb.179.1.235-242.1997;
RA   Kawasaki S., Arai H., Kodama T., Igarashi Y.;
RT   "Gene cluster for dissimilatory nitrite reductase (nir) from Pseudomonas
RT   aeruginosa: sequencing and identification of a locus for heme d1
RT   biosynthesis.";
RL   J. Bacteriol. 179:235-242(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Involved in heme d1 biosynthesis (PubMed:8982003). Catalyzes
CC       the decarboxylation of siroheme into didecarboxysiroheme (By
CC       similarity). {ECO:0000250|UniProtKB:I6UH61,
CC       ECO:0000269|PubMed:8982003}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2;
CC         Xref=Rhea:RHEA:19093, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:60052, ChEBI:CHEBI:140497; EC=4.1.1.111;
CC         Evidence={ECO:0000250|UniProtKB:I6UH61};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism.
CC       {ECO:0000305|PubMed:8982003}.
CC   -!- SUBUNIT: Probably forms a complex composed of NirD, NirL, NirG and
CC       NirH. All proteins are required for the total conversion of siroheme to
CC       didecarboxysiroheme. {ECO:0000250|UniProtKB:I6UH61}.
CC   -!- DISRUPTION PHENOTYPE: The nirDLGH mutant lacks dissimilatory nitrite
CC       reductase (NIR) activity. The NIR activity is restored by adding
CC       purified heme d1. {ECO:0000269|PubMed:8982003}.
CC   -!- SIMILARITY: Belongs to the Ahb/Nir family. {ECO:0000305}.
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DR   EMBL; D84475; BAA12678.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG03903.1; -; Genomic_DNA.
DR   PIR; F83581; F83581.
DR   RefSeq; NP_249205.1; NC_002516.2.
DR   RefSeq; WP_003111534.1; NZ_QZGE01000010.1.
DR   AlphaFoldDB; P95413; -.
DR   SMR; P95413; -.
DR   STRING; 287.DR97_3482; -.
DR   PaxDb; P95413; -.
DR   PRIDE; P95413; -.
DR   DNASU; 879762; -.
DR   EnsemblBacteria; AAG03903; AAG03903; PA0514.
DR   GeneID; 879762; -.
DR   KEGG; pae:PA0514; -.
DR   PATRIC; fig|208964.12.peg.544; -.
DR   PseudoCAP; PA0514; -.
DR   HOGENOM; CLU_112007_0_1_6; -.
DR   OMA; NLFCMVH; -.
DR   PhylomeDB; P95413; -.
DR   BioCyc; PAER208964:G1FZ6-519-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IMP:PseudoCAP.
DR   InterPro; IPR040523; AsnC_trans_reg2.
DR   Pfam; PF17805; AsnC_trans_reg2; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..174
FT                   /note="Siroheme decarboxylase NirL subunit"
FT                   /id="PRO_0000287796"
SQ   SEQUENCE   174 AA;  20210 MW;  97DC499DC3AED900 CRC64;
     MNPVEPLAAP QRQHLRYLLE QGLPLASRPY RVLAERIGAG EDEVLEQVRR WDEDGLFRRF
     GVILHHRALG YTANAMLVLD VADAEVDAVG RALAHETIVS LCYRRPRRLP MWPYNLFCMI
     HGRERGEVER QIEALLERHA LRQTPHRWLF SLRAYKQCGG RYTAPPADLE RRHG