ID A2SFK2_METPP Unreviewed; 426 AA.
AC A2SFK2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Ergothioneine biosynthesis protein EgtB {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Mpe_A1379 {ECO:0000313|EMBL:ABM94341.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM94341.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM94341.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037882}.
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DR EMBL; CP000555; ABM94341.1; -; Genomic_DNA.
DR AlphaFoldDB; A2SFK2; -.
DR STRING; 420662.Mpe_A1379; -.
DR KEGG; mpt:Mpe_A1379; -.
DR eggNOG; COG1262; Bacteria.
DR HOGENOM; CLU_012431_9_0_4; -.
DR Proteomes; UP000000366; 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); 2.
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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366}.
FT DOMAIN 26..162
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 212..345
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
SQ SEQUENCE 426 AA; 47506 MW; 4BD2DDE52DBCA4EB CRC64;
MNSRVAELSS SAPSVDRSLR IVWRRRLEAV RSQSLQLAAP LSAEDRCVQS MPDASPTKWH
LAHTTWFFET VVLQAHQPGY RVHDERYAFL FNSYYESLGP RHPRAQRGLL TRPSNEEVLQ
YRRHVDEAML TFVRESDDAA WLAALPLIAL GLQHEQQHQE LMLTDAKHLL SLNPLQPGYR
SASPDGEGRV FAARGLHPAP VCGPPLRWLA RAGGIADIGA PSTTAFAFDN ETPCHRALLQ
AHELASRPVA NREFLEFMRD GGYRRPELWL SDGWAAVQQQ GWAAPLYWSD TEARCPGVFT
LLGPRALDLD EPVSHLSFYE AAAYATWAGA RLPTEFEWEA AAADGVLEGT GEVWEWTRSS
YDPYPGFRPQ AGAVAEYNGK FMVGQLVLRG GSCATPSGHA RPSYRNFFAP GARWQFAGLR
LARDVS
//
