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Database: UniProt
Entry: A0A1B9EHR6_9ACTN
LinkDB: A0A1B9EHR6_9ACTN
Original site: A0A1B9EHR6_9ACTN 
ID   A0A1B9EHR6_9ACTN        Unreviewed;       439 AA.
AC   A0A1B9EHR6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-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   Name=cysG {ECO:0000313|EMBL:OCC07206.1};
GN   ORFNames=A3Q37_07030 {ECO:0000313|EMBL:OCC07206.1};
OS   Streptomyces sp. PTY087I2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1819298 {ECO:0000313|EMBL:OCC07206.1, ECO:0000313|Proteomes:UP000093256};
RN   [1] {ECO:0000313|EMBL:OCC07206.1, ECO:0000313|Proteomes:UP000093256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PTY087I2 {ECO:0000313|EMBL:OCC07206.1,
RC   ECO:0000313|Proteomes:UP000093256};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879, ECO:0000256|RuleBase:RU003960}.
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:OCC07206.1}.
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DR   EMBL; LZRD01000062; OCC07206.1; -; Genomic_DNA.
DR   RefSeq; WP_065491107.1; NZ_LZRD01000062.1.
DR   AlphaFoldDB; A0A1B9EHR6; -.
DR   PATRIC; fig|1819298.4.peg.7280; -.
DR   Proteomes; UP000093256; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:InterPro.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:InterPro.
DR   CDD; cd11642; SUMT; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006366; CobA/CysG_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR012409; Sirohaem_synth.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR   PANTHER; PTHR45790:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF13241; NAD_binding_7; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036426; Sirohaem_synth; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU003960};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093256};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          191..402
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        221
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT   ACT_SITE        243
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ   SEQUENCE   439 AA;  45978 MW;  52403A97A27FD5A1 CRC64;
     MAEHADHADR SGHADHADRA GHTDHPAYPV GLRLHGRRVV VIGGGQVAQR RLPQLIATGA
     VITLISPSAT PSVEAMADAG EIRWERRRYR DGDLADTWYA LVASSDTTAN DAASVEAERT
     RTWCVRSDDA EAATAWTPAT GRIENITVAV LNTTPRGRDP RHSAALRDAI VEGLRDGTLA
     APHHRTRAPG VALVGGGPGD PDLITVRGRR LLAEADVVIA DRLGPRDLLD ELPPHVEVID
     AAKIPYGRFM AQEAINQALI EHAKAGKSVV RLKGGDPFVF GRGMEEAQAL AAEGIPCTVV
     PGISSTISVP GAAGIPVTHR GVAHEFTVVS GHVAPEDPRS LVDWEAIARL RGTLVLLMAV
     DKIGAIAAAL IAHGKDPATP VALVQEGTTA AQRRVDATLA DVGERAVAED VRPPAVIVIG
     DVVAVGPDSA PAPVQDAAE
//
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