GenomeNet

Database: UniProt
Entry: A0A0M9CCJ9_9ACTN
LinkDB: A0A0M9CCJ9_9ACTN
Original site: A0A0M9CCJ9_9ACTN 
ID   A0A0M9CCJ9_9ACTN        Unreviewed;       584 AA.
AC   A0A0M9CCJ9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=uroporphyrinogen-III C-methyltransferase {ECO:0000256|ARBA:ARBA00012162};
DE            EC=2.1.1.107 {ECO:0000256|ARBA:ARBA00012162};
GN   ORFNames=ISGA_08485 {ECO:0000313|EMBL:KOY49706.1};
OS   Gordonia sp. NB41Y.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=875808 {ECO:0000313|EMBL:KOY49706.1, ECO:0000313|Proteomes:UP000011989};
RN   [1] {ECO:0000313|EMBL:KOY49706.1, ECO:0000313|Proteomes:UP000011989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB4-1Y {ECO:0000313|EMBL:KOY49706.1,
RC   ECO:0000313|Proteomes:UP000011989};
RX   PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA   Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT   "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT   to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL   Microbiology 159:1618-1628(2013).
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOY49706.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; APHK02000050; KOY49706.1; -; Genomic_DNA.
DR   RefSeq; WP_053777002.1; NZ_CP132196.1.
DR   AlphaFoldDB; A0A0M9CCJ9; -.
DR   STRING; 1241906.ISGA_08485; -.
DR   OrthoDB; 9815856at2; -.
DR   Proteomes; UP000011989; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0033014; P:tetrapyrrole biosynthetic process; IEA:InterPro.
DR   CDD; cd06578; HemD; 1.
DR   Gene3D; 3.40.50.10090; -; 2.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR   InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   PANTHER; PTHR45790:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF02602; HEM4; 1.
DR   Pfam; PF00590; TP_methylase; 2.
DR   SUPFAM; SSF69618; HemD-like; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KOY49706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011989};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOY49706.1}.
FT   DOMAIN          13..85
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   DOMAIN          119..277
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   DOMAIN          326..556
FT                   /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT                   synthase"
FT                   /evidence="ECO:0000259|Pfam:PF02602"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   584 AA;  61473 MW;  E3A19A110202CBB0 CRC64;
     MSRTTKKANP GRILFVGSGP GDPDLLTVRA RSVITSATTA YVDPDVPATV VAMIGADHRE
     QPADDQRRST SKAKKDQAAK DQAKADATTT DDATSSTGAD ATTGDAKAPD AKAADTKSAE
     KSAEEPEDQI VRPALGDPSE VAKTLVAAAK AGDDVVRVVS GDPLTTDSVL AEVNAVARTS
     VTFEVLPGLP AASVVPSYAG MPLGSRHTEA DVRAEGVDWA ALAAAPGPLV LHATSGHLAE
     TASALTEHGL APQTPVAITI NGTTCAQRTI EATLATLNEQ GNALTGPLIL TIGQVVTQRG
     KLSWWESRAL YGWTVLVPRT KDQAADMSDR LVSHGAIPKE VPTIAVEPPR SPAQMERAVK
     GLVDGRYQWV VFTSTNSVRA VWEKFAEFGL DARAFSGVKI ACVGEATAAK VRAFGINPEL
     VPSGEQSSLG LLEDFPPYDD VFDPVDRILL PRADIATETL SEGLRERGWE IDDVTAYRTV
     RAAPPPAQTR EMIKTGGFDA VCFTSSSTVR NLVGIAGKPH ARTIVACIGP KTAETATEFG
     LRVDVQPENA SVTELVDALA EHAARLRAEG ALPPPRKKTR RSRS
//
DBGET integrated database retrieval system