ID V2Y9R7_MONRO Unreviewed; 602 AA.
AC V2Y9R7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN ORFNames=Moror_14746 {ECO:0000313|EMBL:ESK88424.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK88424.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK88424.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK88424.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:ESK88424.1}.
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DR EMBL; AWSO01000650; ESK88424.1; -; Genomic_DNA.
DR RefSeq; XP_007852291.1; XM_007854100.1.
DR AlphaFoldDB; V2Y9R7; -.
DR STRING; 1381753.V2Y9R7; -.
DR KEGG; mrr:Moror_14746; -.
DR HOGENOM; CLU_011276_11_1_1; -.
DR OrthoDB; 296644at2759; -.
DR Proteomes; UP000017559; 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 NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
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:UP000017559};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT DOMAIN 168..191
FT /note="Siroheme synthase central"
FT /evidence="ECO:0000259|Pfam:PF14824"
FT DOMAIN 248..285
FT /note="Siroheme biosynthesis protein Met8 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14823"
FT DOMAIN 314..531
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 229..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 65143 MW; E2C7F77A68D276B3 CRC64;
MGFPTPQPGA SLILSFPLQK KTTVLLGSGM LAASRAFAAL EAGSAVVILS HGGTTTACDE
LKWRAEYGQV TVVDFDSLPC SSTVAEENKD VEALDHFLKA THTDISFVCI TDTISGSPFR
RSRQSAEKLY SLCKAKKILV NTTDMPDLCD FSFTSNHRFE DSSGAKAPLQ VGVTTNGQGC
RLAGRIRREI VGKLPKEVGL AVEKVGKMRA LAKAGEDFEV ADANEDCFED TGVTTPNRPV
PQRSKTETAS ERAKRRMKWV AQISEYWSIQ RLSKLTEEEM GEILSGEHGA DDREESVPIP
SIHSLTLQPP VGRILLVGSG PGHPSLLTLA THTALTKLAH LVLSDKLVPD AVLALIPSHV
DVRIAKKFPG NAEGAQNEMM EAAVEAAKRG LTVVRLKQGD PVVYGRAGEE VLYFRERGFE
PVVVPGVTSA IAAPTFAGIP VTQRGVAESF FVCTGVGRKG KEVQLPGYER GRTLVILMGV
ARLSQVVSTL LALEEGHQRI GKAYPPHTPI AIIERASMPD QRVLESTLKD VVQALENLGE
QRPPGMIIVG WVVLALWRTG NVNVLDEGAE NRDAERVIQW LGGPDAPGWR VREGLSDEWE
SL
//
