ID A0A345XN83_9ACTN Unreviewed; 559 AA.
AC A0A345XN83;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Bifunctional uroporphyrinogen-III C-methyltransferase/uroporphyrinogen-III synthase {ECO:0000313|EMBL:AXK33099.1};
GN ORFNames=DVA86_10990 {ECO:0000313|EMBL:AXK33099.1};
OS Streptomyces armeniacus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK33099.1, ECO:0000313|Proteomes:UP000254425};
RN [1] {ECO:0000313|EMBL:AXK33099.1, ECO:0000313|Proteomes:UP000254425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK33099.1,
RC ECO:0000313|Proteomes:UP000254425};
RA Labana P., Gosse J.T., Boddy C.N.;
RT "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005879}.
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DR EMBL; CP031320; AXK33099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345XN83; -.
DR Proteomes; UP000254425; Chromosome.
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 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; 1.
DR SUPFAM; SSF69618; HemD-like; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AXK33099.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254425};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AXK33099.1}.
FT DOMAIN 21..233
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 292..522
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
FT REGION 60..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 58514 MW; D355CC2A50D62C99 CRC64;
MSPTAAQSST TQHLYGAHGH VTFLGAGPGD PGLLTLSAVE ALARADVLVA DPQVHGIVRP
HARAGVDTPL RGAEQPDPTG QASTAHAATG DWANIVMAAA RSGKRVVRAV VGDPGLDADA
AQEMLACVAE GITFEVVPGV ATAVGVPAYA GVPLRDAQGT DVRFIDARTA DDRCWTESGA
SDATLVVSVA LDSVAAAAGE LVAAGRKPDT PLSVTLAGTT TRQRTWTATL GSIAQTLKAA
KVLPSSDGGQ PVIAVVGERS APAHREQLAW FESKPLFGWQ VLVPRTKEQA ASLSDQLRSY
GAVPAEVPTI AVEPPRTPQQ MERAVKGLVT GRYEWIAFTS VNAVKAVREK FEEYGLDARA
FAGIKVAAVG EQTAAALVEF GVKPDLVPSG EQSAAGLLED WPPYDPVFDP IDRVFLPRAD
IATETLVAGL IELGWEVDDV TAYRTVRASP PPAETREAIK GGGFDAVLFT SSSTVRNLVG
IAGKPHNVTI IACIGPATAK TAEEHGLRVD VLSPEPSVHK LAEALADYGQ KRRSEAAEAG
EPVKRPSEKR PTRRRARTS
//