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Database: UniProt
Entry: A0A2G8SC14_9APHY
LinkDB: A0A2G8SC14_9APHY
Original site: A0A2G8SC14_9APHY 
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}.
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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
//
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