ID   NIRG_PSEST              Reviewed;         147 AA.
AC   Q52524;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Siroheme decarboxylase NirG subunit {ECO:0000250|UniProtKB:I6TCK3};
DE            EC=4.1.1.111 {ECO:0000250|UniProtKB:I6TCK3};
GN   Name=nirG {ECO:0000303|PubMed:7588711};
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC   568 / 218 / ZoBell 632;
RX   PubMed=7588711; DOI=10.1111/j.1432-1033.1995.tb20868.x;
RA   Palmedo G., Seither P., Koerner H., Matthews J.C., Burkhalter R.S.,
RA   Timkovich R., Zumft W.G.;
RT   "Resolution of the nirD locus for heme d1 synthesis of cytochrome cd1
RT   (respiratory nitrite reductase) from Pseudomonas stutzeri.";
RL   Eur. J. Biochem. 232:737-746(1995).
CC   -!- FUNCTION: Involved in heme d1 biosynthesis. Catalyzes the
CC       decarboxylation of siroheme into didecarboxysiroheme.
CC       {ECO:0000250|UniProtKB:I6TCK3}.
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:I6TCK3};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism.
CC       {ECO:0000250|UniProtKB:I6TCK3}.
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:I6TCK3}.
CC   -!- DISRUPTION PHENOTYPE: Insertional mutagenesis results in the loss of
CC       respiratory nitrite reductase activity in vivo and in vitro. Mutant
CC       strains synthesize a periplasmic cytochrome cd1 that lacks heme d1.
CC       {ECO:0000269|PubMed:7588711}.
CC   -!- SIMILARITY: Belongs to the Ahb/Nir family. {ECO:0000305}.
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DR   EMBL; X53676; CAA90581.1; -; Genomic_DNA.
DR   PIR; S68351; S68351.
DR   RefSeq; WP_003279931.1; NZ_CP036186.1.
DR   AlphaFoldDB; Q52524; -.
DR   SMR; Q52524; -.
DR   STRING; 32042.PstZobell_00927; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000485; AsnC-type_HTH_dom.
DR   InterPro; IPR040523; AsnC_trans_reg2.
DR   InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR   InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF17805; AsnC_trans_reg2; 1.
DR   Pfam; PF13404; HTH_AsnC-type; 1.
DR   SMART; SM00344; HTH_ASNC; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..147
FT                   /note="Siroheme decarboxylase NirG subunit"
FT                   /id="PRO_0000021816"
SQ   SEQUENCE   147 AA;  16566 MW;  F64080056B42EBD6 CRC64;
     MDELDRQLIN RLQHGLPLVR HPWEALAEEL GSTAEVLRLR VQALLDDGTL TRFGPMFDID
     RLGGAFTLAA LSVPEARFDA VAAQLEAMPE VAHNYRREHQ WNMWFVLGCE TPQGITETIA
     RIEAQTGLTV LNLPKEETFH VGLHFPV