HUGZ_HELPY
ID HUGZ_HELPY Reviewed; 251 AA.
AC O25087;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Heme oxygenase HugZ {ECO:0000305};
DE EC=1.14.99.- {ECO:0000269|PubMed:19091096};
GN Name=hugZ {ECO:0000303|PubMed:19091096};
GN OrderedLocusNames=HP_0318 {ECO:0000312|EMBL:AAD07387.1};
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, HEME-BINDING, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=19091096; DOI=10.1186/1471-2180-8-226;
RA Guo Y., Guo G., Mao X., Zhang W., Xiao J., Tong W., Liu T., Xiao B.,
RA Liu X., Feng Y., Zou Q.;
RT "Functional identification of HugZ, a heme oxygenase from Helicobacter
RT pylori.";
RL BMC Microbiol. 8:226-226(2008).
RN [3]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=19342784; DOI=10.1107/s1744309109008094;
RA Jiang F., Hu Y., Guo Y., Guo G., Zou Q.M., Wang D.C.;
RT "Crystallization and preliminary crystallographic studies of Helicobacter
RT pylori HugZ, a novel haem oxygenase.";
RL Acta Crystallogr. F 65:376-378(2009).
RN [4] {ECO:0007744|PDB:3GAS}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION,
RP HEME-BINDING, SUBUNIT, AND MUTAGENESIS OF ARG-166 AND HIS-245.
RX PubMed=21030596; DOI=10.1074/jbc.m110.172007;
RA Hu Y., Jiang F., Guo Y., Shen X., Zhang Y., Zhang R., Guo G., Mao X.,
RA Zou Q., Wang D.C.;
RT "Crystal structure of HugZ, a novel heme oxygenase from Helicobacter
RT pylori.";
RL J. Biol. Chem. 286:1537-1544(2011).
CC -!- FUNCTION: Involved in heme iron utilization (PubMed:19091096,
CC PubMed:21030596). Catalyzes the degradation of heme to biliverdin, with
CC the release of iron and carbon monoxide (PubMed:19091096,
CC PubMed:21030596). Release of iron from heme may play a crucial role in
CC the pathogenicity of H.pylori (PubMed:19091096).
CC {ECO:0000269|PubMed:19091096, ECO:0000269|PubMed:21030596}.
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;
CC Evidence={ECO:0000269|PubMed:19091096};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19342784,
CC ECO:0000269|PubMed:21030596}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19091096}.
CC -!- INDUCTION: Down-regulated by iron. {ECO:0000269|PubMed:19091096}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant cannot utilize heme iron for
CC normal growth. {ECO:0000269|PubMed:19091096}.
CC -!- SIMILARITY: Belongs to the heme oxygenase HugZ/HutZ family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD07387.1; -; Genomic_DNA.
DR PIR; F64559; F64559.
DR RefSeq; NP_207116.1; NC_000915.1.
DR RefSeq; WP_000934548.1; NC_018939.1.
DR PDB; 3GAS; X-ray; 1.80 A; A/B/C/D/E/F=1-251.
DR PDBsum; 3GAS; -.
DR AlphaFoldDB; O25087; -.
DR SMR; O25087; -.
DR STRING; 85962.C694_01610; -.
DR PaxDb; O25087; -.
DR EnsemblBacteria; AAD07387; AAD07387; HP_0318.
DR KEGG; hpy:HP_0318; -.
DR PATRIC; fig|85962.47.peg.340; -.
DR eggNOG; COG0748; Bacteria.
DR OMA; NNPHNVE; -.
DR PhylomeDB; O25087; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070967; F:coenzyme F420 binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR Gene3D; 2.30.110.10; -; 1.
DR Gene3D; 3.20.180.10; -; 1.
DR InterPro; IPR019595; DUF2470.
DR InterPro; IPR037119; Haem_oxidase_HugZ-like_sf.
DR InterPro; IPR026324; Haem_oxygenase_HugZ.
DR InterPro; IPR011576; Pyridox_Oxase_put.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF10615; DUF2470; 1.
DR Pfam; PF01243; Putative_PNPOx; 1.
DR TIGRFAMs; TIGR04109; heme_ox_HugZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Virulence.
FT CHAIN 1..251
FT /note="Heme oxygenase HugZ"
FT /id="PRO_0000446444"
FT BINDING 245
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21030596"
FT MUTAGEN 166
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21030596"
FT MUTAGEN 245
FT /note="H->A,Q: Increase in activity."
FT /evidence="ECO:0000269|PubMed:21030596"
FT MUTAGEN 245
FT /note="H->N: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:21030596"
SQ SEQUENCE 251 AA; 28507 MW; 54E62CE29F672B26 CRC64;
MLNRIIEHMN AHHVEDMKGL LKKFGQVHHA ENVAFKSVDP QGIVIGYNHN QTLRIEFNHE
VKDPKDYKNA IIELCQSVEK THDLKGVEEE VKAFKESFDS VCLATLHPNG HVVCSYAPLM
SDGKQYYIYV SEVAEHFAGL KNNPHNVEVM FLEDESKAKS AILRKRLRYK TNARFIERGA
EFDKAFDSFI EKTGGAGGIK TIRAMQDFHL IALDFKEGRF VKGFGQAYDI LGDKIAYVGD
KGNPHNFAHK K
