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Database: UniProt
Entry: A1KT33_NEIMF
LinkDB: A1KT33_NEIMF
Original site: A1KT33_NEIMF 
ID   A1KT33_NEIMF            Unreviewed;       103 AA.
AC   A1KT33;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN   OrderedLocusNames=NMC0726 {ECO:0000313|EMBL:CAM10015.1};
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831 {ECO:0000313|EMBL:CAM10015.1, ECO:0000313|Proteomes:UP000002286};
RN   [1] {ECO:0000313|EMBL:CAM10015.1, ECO:0000313|Proteomes:UP000002286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18
RC   {ECO:0000313|Proteomes:UP000002286};
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC       {ECO:0000256|ARBA:ARBA00009630, ECO:0000256|PIRNR:PIRNR005894}.
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DR   EMBL; AM421808; CAM10015.1; -; Genomic_DNA.
DR   RefSeq; WP_002214004.1; NC_008767.1.
DR   AlphaFoldDB; A1KT33; -.
DR   GeneID; 83617033; -.
DR   KEGG; nmc:NMC0726; -.
DR   HOGENOM; CLU_026126_2_1_4; -.
DR   Proteomes; UP000002286; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03028; GRX_PICOT_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR014434; Monothiol_GRX.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 1.
DR   PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR10293:SF72; MONOTHIOL GLUTAREDOXIN-S14, CHLOROPLASTIC; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PIRSF; PIRSF005894; Monothiol_GRX; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR005894-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR005894-2};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR005894-
KW   2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR005894-2}.
FT   DOMAIN          17..82
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   BINDING         30
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-2"
SQ   SEQUENCE   103 AA;  11524 MW;  599B954E95F9D6DF CRC64;
     MASIHDQIKE VVTTHRVVLF MKGTKQFPQC GFSSRAVQIL NAAGCTDYVT VNVLENPEVR
     QGIKEYSDWP TIPQLYVNGE FVGGSDILME MYEAGELQEL LKA
//
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