ID A0A2G8SC14_9APHY Unreviewed; 613 AA.
AC A0A2G8SC14;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN ORFNames=GSI_05997 {ECO:0000313|EMBL:PIL31299.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL31299.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL31299.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL31299.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|RuleBase:RU003960}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the precorrin
CC methyltransferase family. {ECO:0000256|ARBA:ARBA00035662}.
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:PIL31299.1}.
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; AYKW01000012; PIL31299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8SC14; -.
DR STRING; 1077348.A0A2G8SC14; -.
DR OrthoDB; 296644at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR028162; Met8_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028281; Sirohaem_synthase_central.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR PANTHER; PTHR45790:SF6; UROPORPHYRINOGEN-III C-METHYLTRANSFERASE; 1.
DR Pfam; PF13241; NAD_binding_7; 1.
DR Pfam; PF14823; Sirohm_synth_C; 1.
DR Pfam; PF14824; Sirohm_synth_M; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR PROSITE; PS00840; SUMT_2; 1.
PE 3: Inferred from homology;
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU003960}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT DOMAIN 172..196
FT /note="Siroheme synthase central"
FT /evidence="ECO:0000259|Pfam:PF14824"
FT DOMAIN 247..287
FT /note="Siroheme biosynthesis protein Met8 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14823"
FT DOMAIN 325..545
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 215..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 66310 MW; 689BE898C46B4E75 CRC64;
MEAFPRPVGG ASLLVAFRPV RRTVIVVGGN TLAASRAFAA LQAEAKVLVV VRGGLEGACE
ELRWRAGQKQ LELLDFDTLP TSQARPEDFW RDGKALDTFI YQLPTKPAMV CVTDTVVGPT
GYRRCYDAAF AIARECRHRQ IPITVADIPD LCDFTFLSTH RFPSSETGSA SPLQVGVTTN
GHGCRLAGRI RRDIVASLPK DVGGAVEKVG QLRMQAKESQ GDGEGQDLNE DGAPVTPNEP
VPQRKLEETE KDRGRRRMKW VAQVSEYWPI RRLAQMSDED MAAVLDGREG LRGTTPPSTG
DPSHAEGNTT TPVHGLVLSP PRRGRIFLVG SGPGHPSLLT VATHAALTKH TQLVLSDKLV
PDAVLALIPP GVEVRIARKF PGNADGAQQE LMEAAVEAAK RGLTVVRLKQ GDPTVYGRAG
EEVLYFRAHG FEPVVVPGVS SVLAGPTFAG IPVTQRGAAE SFVVCTGVGR AGKEVKLPGY
DRGRTLVILM GVARLPQVLE TLQSDDAGAI KRRDGRAYPS STPIALIERA SMPDQRVIVS
TLRDITTALD TVGEQRPPGM LVIGWSIPSL WEKGDVNILD EGAEARDEER VRTWLGGKLW
RVTEGIEAGW EDW
//