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Database: UniProt
Entry: A0A1H9IT96_9ACTN
LinkDB: A0A1H9IT96_9ACTN
Original site: A0A1H9IT96_9ACTN 
ID   A0A1H9IT96_9ACTN        Unreviewed;       410 AA.
AC   A0A1H9IT96;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000313|EMBL:SEQ77732.1};
GN   ORFNames=SAMN04487983_100820 {ECO:0000313|EMBL:SEQ77732.1};
OS   Streptomyces sp. yr375.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761906 {ECO:0000313|EMBL:SEQ77732.1, ECO:0000313|Proteomes:UP000198568};
RN   [1] {ECO:0000313|EMBL:SEQ77732.1, ECO:0000313|Proteomes:UP000198568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR375 {ECO:0000313|EMBL:SEQ77732.1,
RC   ECO:0000313|Proteomes:UP000198568};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin;
CC         Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827; EC=1.3.1.76;
CC         Evidence={ECO:0000256|ARBA:ARBA00001156};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005010}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879, ECO:0000256|RuleBase:RU003960}.
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DR   EMBL; FOFF01000008; SEQ77732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9IT96; -.
DR   STRING; 1761906.SAMN04487983_100820; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00262; UER00222.
DR   Proteomes; UP000198568; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
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:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR006367; Sirohaem_synthase_N.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR   NCBIfam; TIGR01470; cysG_Nterm; 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:UP000198568};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          170..381
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ   SEQUENCE   410 AA;  42961 MW;  6D10965959B1DBE6 CRC64;
     MAEHPAYPVG LRLTGRRVVV LGGGQVAQRR LPALIAAGAA VHLVSPEATP SVEAMADAGE
     ITWTRRAYAE GDLADAWYAL IATRDPEANA RASAEAEQHR VWCVRSDDAD QATAWTPATG
     HSEGVTVAVL TTDARGRDPR HTAAIRDAVV EGLRDGTLVA PHHRTRTPGV ALVGGGPGDP
     DLITVRGRRL LAEADVVIAD RLGPRDLLAE LPPHVEVIDA AKIPYGRFMA QEAINNALIE
     HARQGKSVVR LKGGDPYVFG RGMEELQALA EAGIACTVVP GISSSISVPG AAGIPVTHRG
     VAHEFTVVSG HVAPDDERSL VDWPSLAKLT GTLVILMGVD KIGKIAETLV AHGKSPDTPV
     ALVQEGTTAA QRRVDATLAT VAETVRAEEV RPPAVIVVGA VVTVGSRTFE
//
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