ID Q4QMX3_HAEI8 Unreviewed; 241 AA.
AC Q4QMX3;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Peroxiredoxin/glutaredoxin {ECO:0000313|EMBL:AAX87624.1};
GN Name=pdgX {ECO:0000313|EMBL:AAX87624.1};
GN OrderedLocusNames=NTHI0705 {ECO:0000313|EMBL:AAX87624.1};
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310 {ECO:0000313|EMBL:AAX87624.1, ECO:0000313|Proteomes:UP000002525};
RN [1] {ECO:0000313|EMBL:AAX87624.1, ECO:0000313|Proteomes:UP000002525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP {ECO:0000313|EMBL:AAX87624.1,
RC ECO:0000313|Proteomes:UP000002525};
RX PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S.Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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DR EMBL; CP000057; AAX87624.1; -; Genomic_DNA.
DR RefSeq; WP_005649562.1; NC_007146.2.
DR AlphaFoldDB; Q4QMX3; -.
DR PeroxiBase; 4788; HinPrxGrx_86-028NP.
DR GeneID; 72526688; -.
DR KEGG; hit:NTHI0705; -.
DR HOGENOM; CLU_072440_2_2_6; -.
DR Proteomes; UP000002525; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03029; GRX_hybridPRX5; 1.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011906; Glutaredoxin_dom.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02190; GlrX-dom; 1.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 3..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 241 AA; 26727 MW; D3CD532F20EE63EE CRC64;
MSSMEGKKVP QVTFRTRQGD KWVDVTTSEL FDNKTVIVFS LPGAFTPTCS SSHLPRYNEL
APVFKKYGVD DILVVSVNDT FVMNAWKEDE KSENITFIPD GNGEFTEGMG MLVGKEDLGF
GKRSWRYSML VKNGVVEKMF IEPNEPGDPF KVSDADTMLK YLAPQHQVQE SISIFTKPGC
PFCAKAKQLL HDKGLSFEEI ILGHDATIVS VRAVSGRATV PQVFIGGKHI GGSDDLEKYF
A
//
