ID A0A0L0HS25_SPIPD Unreviewed; 635 AA.
AC A0A0L0HS25;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN ORFNames=SPPG_01125 {ECO:0000313|EMBL:KND03654.1};
OS Spizellomyces punctatus (strain DAOM BR117).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Spizellomycetaceae; Spizellomyces.
OX NCBI_TaxID=645134 {ECO:0000313|EMBL:KND03654.1, ECO:0000313|Proteomes:UP000053201};
RN [1] {ECO:0000313|EMBL:KND03654.1, ECO:0000313|Proteomes:UP000053201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM BR117 {ECO:0000313|EMBL:KND03654.1,
RC ECO:0000313|Proteomes:UP000053201};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL Submitted (AUG-2009) 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|RuleBase:RU003960}.
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DR EMBL; KQ257451; KND03654.1; -; Genomic_DNA.
DR RefSeq; XP_016611693.1; XM_016749446.1.
DR AlphaFoldDB; A0A0L0HS25; -.
DR STRING; 645134.A0A0L0HS25; -.
DR GeneID; 27684811; -.
DR VEuPathDB; FungiDB:SPPG_01125; -.
DR eggNOG; KOG1527; Eukaryota.
DR InParanoid; A0A0L0HS25; -.
DR OMA; IPYGRFM; -.
DR OrthoDB; 296644at2759; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000053201; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000103; P:sulfate assimilation; 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; IPR012066; Met1_fungi.
DR InterPro; IPR028162; Met8_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028281; Sirohaem_synthase_central.
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; 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 PIRSF; PIRSF036555; SUMT_yeast; 3.
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; PS00839; SUMT_1; 1.
DR PROSITE; PS00840; SUMT_2; 1.
PE 3: Inferred from homology;
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:UP000053201};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT DOMAIN 130..154
FT /note="Siroheme synthase central"
FT /evidence="ECO:0000259|Pfam:PF14824"
FT DOMAIN 159..223
FT /note="Siroheme biosynthesis protein Met8 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14823"
FT DOMAIN 370..579
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 221..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 67601 MW; C9219ADA6955AF57 CRC64;
MPEPRKVTGG ASFIVGYRLG GKHVLVVGGG KEASGRVFFA LDADARVTVV CPASGLNKDV
ETRVHNGEIV HIDRNFVDSD LDHADMVLSC IDEHDESRRI ATLCRKRRIP VNCADIPELC
DFYFMAQHRN GSLQIGVSTN GCGPRLGARL RDHVVLSLPP RTAEAVDKIG SVRKKIREAD
PDPESSGRRM RWLSRLCDIW SFEEIAALEE DGVLELLDAY ERGDKEPPPP PGRRGENANG
KNGVGDGHED RSAAGLTLIQ YAHSVPLVGA TVDTVASATG SAWNLTTSAV SGSIETASAI
GGHALDITST YARALKETGS AYIQYAVTCT EDIVENGLRL LPEAVSRVAR GTLCLLPLPI
HVSPRPEGGI TLVGAGPGDP GLLTLRALDA IRTADLVVSD QLISDQILAL VPRKRLHLVQ
KKAAGKSDAS QNDANETCLA ALSRGLNVVR LKGGDPFLFG RGGEEVAFFR EKGYEPKIVP
GISSCIAAPE SAFIPVTHRG VADQLLVLSG RGEGGAFPEV PPHYEKRTTV VLMAVGRLQE
LVDRMIEKGY PNDCPAAVVE KGCWRDGSER VVDGTLQTIV GRVKDAAVGA PALLVVGDAV
SVLRSAPVEE PQGFITDGTI SHSSGEINGA MVEHN
//
