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Database: UniProt
Entry: A0A1I7ELG7_9BURK
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Original site: A0A1I7ELG7_9BURK 
ID   A0A1I7ELG7_9BURK        Unreviewed;       673 AA.
AC   A0A1I7ELG7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Uroporphyrinogen III methyltransferase / synthase {ECO:0000313|EMBL:SFU24745.1};
GN   ORFNames=SAMN05192563_102954 {ECO:0000313|EMBL:SFU24745.1};
OS   Paraburkholderia aspalathi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1324617 {ECO:0000313|EMBL:SFU24745.1, ECO:0000313|Proteomes:UP000198844};
RN   [1] {ECO:0000313|EMBL:SFU24745.1, ECO:0000313|Proteomes:UP000198844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 27731 {ECO:0000313|EMBL:SFU24745.1,
RC   ECO:0000313|Proteomes:UP000198844};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FPBH01000029; SFU24745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7ELG7; -.
DR   OrthoDB; 9787650at2; -.
DR   Proteomes; UP000198844; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR   InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
DR   InterPro; IPR007470; HemX.
DR   PANTHER; PTHR38043; PROTEIN HEMX; 1.
DR   PANTHER; PTHR38043:SF1; PROTEIN HEMX; 1.
DR   Pfam; PF02602; HEM4; 1.
DR   Pfam; PF04375; HemX; 1.
DR   SUPFAM; SSF69618; HemD-like; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000313|EMBL:SFU24745.1};
KW   Transferase {ECO:0000313|EMBL:SFU24745.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        343..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..267
FT                   /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT                   synthase"
FT                   /evidence="ECO:0000259|Pfam:PF02602"
FT   REGION          287..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          405..432
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        289..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  71521 MW;  81D7D522FCFB2862 CRC64;
     MAADIPGNAS SSVDKAAFTV VITRPAGQSN ELIAQLAAAG VAVLDFPLID IAPVTDEAPL
     RAALASLERY ALVVFVSPNA VDHAFARSDA IWPHALPIGV VGPGSVQALA RHGVAAPAYT
     IISPPSVADD DTARFDSEGL FAAIDTALGA TSLEGKRVLI VRGDGGREWL ADRLREAGAE
     VETVAAYRRL VPEPSIGGWA RVHALLAGAP HAWLLTSSEG VRNLHELAQE HLTADEITQL
     KHANLVTPHP RIAQTARALG FDSITVSGAG DERIARALLA AVPTVVQPVP SNPAHSPAKS
     RMTETNASTN ASPQPAATTA LPPNPPFTPY EAQEKRRSAS GPLLWFVVVI IACAAGVGGY
     ALNRKVERTE QQLVQRQQAN DAQTNDLRVK TDQALATVHQ SDSQVAQLEG KLADAQTAQQ
     ALQQQYSDLA RNRDDWTMAE VGQMLSAASQ QLQLTGNTQL ALFALQSADT RLAASDSPQA
     VTVRKAIAQD IDKLKAAPST DLTGMAIKLD NAIDQVDSLP LSGEAPIAHA TPKAATWADT
     AKVAAATGEP RWKVWWREVT TGIGQQLTSL VQVRRIDNAD AMLVTPDQGY FVRENLKLRL
     LSARLALLSR NQTTLKSDLQ AAQAALTRYF DNTSKKTQTV VDLVKQVDAG SAAVELPTLN
     TSLQAVNQYR SRG
//
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