PIGA_PSEAE
ID PIGA_PSEAE Reviewed; 198 AA.
AC G3XCZ8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Heme oxygenase PigA {ECO:0000305};
DE EC=1.14.99.58 {ECO:0000269|PubMed:11591684, ECO:0000269|PubMed:12475329};
GN Name=pigA {ECO:0000303|PubMed:11591684};
GN OrderedLocusNames=PA0672 {ECO:0000312|EMBL:AAG04061.1};
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 [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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=IA614 / PAO1;
RX PubMed=11591684; DOI=10.1128/jb.183.21.6394-6403.2001;
RA Ratliff M., Zhu W., Deshmukh R., Wilks A., Stojiljkovic I.;
RT "Homologues of neisserial heme oxygenase in Gram-negative bacteria:
RT degradation of heme by the product of the pigA gene of Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 183:6394-6403(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASN-19 AND PHE-117.
RX PubMed=12475329; DOI=10.1021/ja0274960;
RA Caignan G.A., Deshmukh R., Wilks A., Zeng Y., Huang H.W., Moenne-Loccoz P.,
RA Bunce R.A., Eastman M.A., Rivera M.;
RT "Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa
RT heme oxygenase as a consequence of an unusual seating of the heme.";
RL J. Am. Chem. Soc. 124:14879-14892(2002).
RN [4] {ECO:0007744|PDB:1SK7}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=15122889; DOI=10.1021/bi049687g;
RA Friedman J., Lad L., Li H., Wilks A., Poulos T.L.;
RT "Structural basis for novel delta-regioselective heme oxygenation in the
RT opportunistic pathogen Pseudomonas aeruginosa.";
RL Biochemistry 43:5239-5245(2004).
CC -!- FUNCTION: Involved in heme degradation. Catalyzes the degradation of
CC heme to biliverdin, with the release of iron. Forms biliverdin delta
CC (70%) and beta (30%). {ECO:0000269|PubMed:11591684,
CC ECO:0000269|PubMed:12475329}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 AH2 + 2 H(+) + heme b + 3 O2 = 3 A + biliverdin beta + CO +
CC Fe(2+) + 3 H2O; Xref=Rhea:RHEA:52228, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17245, ChEBI:CHEBI:17499, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:60344, ChEBI:CHEBI:136509; EC=1.14.99.58;
CC Evidence={ECO:0000269|PubMed:11591684, ECO:0000269|PubMed:12475329};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 AH2 + 3 H(+) + heme b + 3 O2 = 3 A + biliverdin delta + CO +
CC Fe(2+) + 3 H2O; Xref=Rhea:RHEA:52224, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17245, ChEBI:CHEBI:17499, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:60344, ChEBI:CHEBI:136510; EC=1.14.99.58;
CC Evidence={ECO:0000269|PubMed:11591684, ECO:0000269|PubMed:12475329};
CC -!- DISRUPTION PHENOTYPE: Mutants are unable to use heme as a source of
CC iron. {ECO:0000269|PubMed:11591684}.
CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG04061.1; -; Genomic_DNA.
DR PIR; A83562; A83562.
DR RefSeq; NP_249363.1; NC_002516.2.
DR RefSeq; WP_003085321.1; NZ_QZGE01000025.1.
DR PDB; 1SK7; X-ray; 1.60 A; A=1-198.
DR PDBsum; 1SK7; -.
DR AlphaFoldDB; G3XCZ8; -.
DR SMR; G3XCZ8; -.
DR STRING; 287.DR97_1447; -.
DR PaxDb; G3XCZ8; -.
DR EnsemblBacteria; AAG04061; AAG04061; PA0672.
DR GeneID; 880820; -.
DR KEGG; pae:PA0672; -.
DR PATRIC; fig|208964.12.peg.703; -.
DR PseudoCAP; PA0672; -.
DR HOGENOM; CLU_085041_1_0_6; -.
DR OMA; EGRGLHW; -.
DR PhylomeDB; G3XCZ8; -.
DR EvolutionaryTrace; G3XCZ8; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071281; P:cellular response to iron ion; EXP:CollecTF.
DR GO; GO:0006788; P:heme oxidation; IMP:PseudoCAP.
DR Gene3D; 1.20.910.10; -; 1.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..198
FT /note="Heme oxygenase PigA"
FT /id="PRO_0000446447"
FT BINDING 26
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:15122889"
FT MUTAGEN 19
FT /note="N->K: No change in regioselectivity of the reaction.
FT Changes regioselectivity and forms biliverdin alpha (55%),
FT biliverdin delta (35%) and biliverdin beta (10%); when
FT associated with Y-117."
FT /evidence="ECO:0000269|PubMed:12475329"
FT MUTAGEN 117
FT /note="F->Y: No change in regioselectivity of the reaction.
FT Changes regioselectivity and forms biliverdin alpha (55%),
FT biliverdin delta (35%) and biliverdin beta (10%); when
FT associated with K-19."
FT /evidence="ECO:0000269|PubMed:12475329"
SQ SEQUENCE 198 AA; 21954 MW; 4308A9BE04B03B95 CRC64;
MDTLAPESTR QNLRSQRLNL LTNEPHQRLE SLVKSKEPFA SRDNFARFVA AQYLFQHDLE
PLYRNEALAR LFPGLASRAR DDAARADLAD LGHPVPEGDQ SVREADLSLA EALGWLFVSE
GSKLGAAFLF KKAAALELDE NFGARHLAEP EGGRAQGWKS FVAILDGIEL NEEEERLAAK
GASDAFNRFG DLLERTFA
