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Database: UniProt
Entry: M4NFS2_9GAMM
LinkDB: M4NFS2_9GAMM
Original site: M4NFS2_9GAMM 
ID   M4NFS2_9GAMM            Unreviewed;       416 AA.
AC   M4NFS2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=TIGR03440 family protein {ECO:0000313|EMBL:AGG89785.1};
DE   Flags: Precursor;
GN   ORFNames=R2APBS1_2706 {ECO:0000313|EMBL:AGG89785.1};
OS   Rhodanobacter denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG89785.1, ECO:0000313|Proteomes:UP000011859};
RN   [1] {ECO:0000313|EMBL:AGG89785.1, ECO:0000313|Proteomes:UP000011859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2APBS1 {ECO:0000313|EMBL:AGG89785.1,
RC   ECO:0000313|Proteomes:UP000011859};
RG   US DOE Joint Genome Institute;
RA   Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Peters L., Pitluck S., Woyke T., Prakash O., Elkins J., Brown S.,
RA   Palumbo A., Hemme C., Zhou J., Watson D., Jardine P., Kostka J., Green S.;
RT   "Complete genome of Rhodanobacter sp. 2APBS1.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037882}.
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DR   EMBL; CP003470; AGG89785.1; -; Genomic_DNA.
DR   RefSeq; WP_015448286.1; NZ_CP088918.1.
DR   AlphaFoldDB; M4NFS2; -.
DR   STRING; 666685.R2APBS1_2706; -.
DR   KEGG; rhd:R2APBS1_2706; -.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_012431_9_0_6; -.
DR   OrthoDB; 9768004at2; -.
DR   Proteomes; UP000011859; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR024775; DinB-like.
DR   InterPro; IPR034660; DinB/YfiT-like.
DR   InterPro; IPR017806; EgtB.
DR   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   NCBIfam; TIGR03440; egtB_TIGR03440; 1.
DR   PANTHER; PTHR23150:SF36; HERCYNINE OXYGENASE; 1.
DR   PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR   Pfam; PF12867; DinB_2; 1.
DR   Pfam; PF03781; FGE-sulfatase; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          15..145
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          187..313
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   DOMAIN          324..412
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
SQ   SEQUENCE   416 AA;  46944 MW;  151D63E0FB99828C CRC64;
     MTTWQSSAPA GIAARFRQVR QCTLALCASL SAEDLQLQSM PDASPGKWHL AHTSWFFEQF
     VLGRDPAYRP RDPAWHYLFN SYYQSVGPMH ARPQRGLLSR PSLDEVLDYR RHVDDAVGEL
     LERSDDAELP GLVELGLQHE QQHQELLLTD IKHAFWCNPL QPAYRAPIAA SADAKVVPLR
     FVDGREGIVE IGHRGEGFAF DHETPRHRAL LQPHALANRL VTNAEYLAFV REGGYREPGL
     WLSDGWATLQ REGWQHPLYW QDDLASEFTL AGARALDPHE PVCHLSYFEA DAFARWAGAR
     LPTEAEWESV AQGVAIDGNL QDAQRFQPRA ASGDAGLLQL YGDVWEWTAS PYVSYPGFRP
     LPGSLGEYNG KFMCGQWVLR GGSCATPRDH VRATYRNFFP PQARWQFAGL RLGQDR
//
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