HEMN_PSEAE
ID HEMN_PSEAE Reviewed; 460 AA.
AC P77915; Q04626; Q04627;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Oxygen-independent coproporphyrinogen III oxidase;
DE Short=CPO;
DE EC=1.3.98.3 {ECO:0000250|UniProtKB:P32131};
DE AltName: Full=Coproporphyrinogen III dehydrogenase;
DE Short=CPDH;
GN Name=hemN; OrderedLocusNames=PA1546;
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].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Savioz A., Zimmermann A., Haas D.;
RT "RpoN-independent promoters having a conserved GG-N10-GC motif in
RT Pseudomonas aeruginosa.";
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9767567; DOI=10.1046/j.1365-2958.1998.00980.x;
RA Rompf A., Hungerer C., Hoffmann T., Lindenmeyer M., Romling U., Gross U.,
RA Doss M.O., Arai H., Igarashi Y., Jahn D.;
RT "Regulation of Pseudomonas aeruginosa hemF and hemN by the dual action of
RT the redox response regulators Anr and Dnr.";
RL Mol. Microbiol. 29:985-997(1998).
RN [3]
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 the heme biosynthesis. Catalyzes the anaerobic
CC oxidative decarboxylation of propionate groups of rings A and B of
CC coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen
CC IX. {ECO:0000269|PubMed:9767567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-
CC deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX;
CC Xref=Rhea:RHEA:15425, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:57307, ChEBI:CHEBI:57309, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789; EC=1.3.98.3;
CC Evidence={ECO:0000250|UniProtKB:P32131};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P32131};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:P32131};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet
CC route): step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P32131}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32131}.
CC -!- INDUCTION: By the redox response regulator Anr under aerobic and
CC anaerobic conditions and by Dnr only under anaerobic conditions.
CC {ECO:0000269|PubMed:9767567}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate
CC coproporphyrinogen-III both under aerobic and anaerobic conditions,
CC however they do not exhibit any obvious growth defects. The hemN hemF
CC double mutant do not abolish aerobic and anaerobic respiratory growth.
CC {ECO:0000269|PubMed:9767567}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25710.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA25711.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA40903.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA40904.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M98276; AAA25710.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M98276; AAA25711.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X57736; CAA40903.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X57736; CAA40904.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X97981; CAA66617.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04935.1; -; Genomic_DNA.
DR PIR; A83454; A83454.
DR RefSeq; NP_250237.1; NC_002516.2.
DR RefSeq; WP_003087267.1; NZ_QZGE01000032.1.
DR AlphaFoldDB; P77915; -.
DR SMR; P77915; -.
DR STRING; 287.DR97_390; -.
DR PaxDb; P77915; -.
DR PRIDE; P77915; -.
DR EnsemblBacteria; AAG04935; AAG04935; PA1546.
DR GeneID; 883053; -.
DR KEGG; pae:PA1546; -.
DR PATRIC; fig|208964.12.peg.1599; -.
DR PseudoCAP; PA1546; -.
DR HOGENOM; CLU_027579_3_0_6; -.
DR InParanoid; P77915; -.
DR OMA; LMCNLEL; -.
DR PhylomeDB; P77915; -.
DR BioCyc; PAER208964:G1FZ6-1574-MON; -.
DR UniPathway; UPA00251; UER00323.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR004558; Coprogen_oxidase_HemN.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR PANTHER; PTHR13932; PTHR13932; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000167; HemN; 1.
DR SFLD; SFLDF00277; oxygen-independent_coproporphy; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00538; hemN; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..460
FT /note="Oxygen-independent coproporphyrinogen III oxidase"
FT /id="PRO_0000109947"
FT DOMAIN 48..287
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 115..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT CONFLICT 104
FT /note="E -> A (in Ref. 1; AAA25710 and 2; CAA66617)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="L -> P (in Ref. 2; CAA66617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 52488 MW; A15EFD0FD04AB03E CRC64;
MLDTIRWDAD LIRRYDLSGP RYTSYPTAVQ FHEGIGPFDQ LHALRDSRKA GHPLSLYVHI
PFCANICYYC ACNKVITKDR GRSAPYLARL VREIEIVSRH LSREQVVEQL HFGGGTPTFL
SPGQLRELMS QLRTHLNLLD DDSGDYGIEI DPREADWSTM GLLRELGFNR VSLGVQDFDM
EVQKAVNRMQ TPEETRTIVE AARTLQYRSI NLDLIYGLPK QTPDSFARTV DEVIALQPDR
LSVFNYAHLP ERFMPQRRIN ADDLPSPGQK LEMLQRTTEQ LAAAGYRYIG MDHFALPDDE
LASAQEDGTL QRNFQGYTTH GHCDLVGLGV SAISQIGDLY SQNSSDINDY QTSLDNGQLA
IRRGLHCNSD DRVRRAVIQQ LICHFELAFE DIETEFGIDF RSYFAELWPD LERFAADGLI
RLDAKGIDIT SSGRLLVRSI CMLFDRYLPS LNRQRFSRVI
