ID A0A2I1GLK4_9GLOM Unreviewed; 1299 AA.
AC A0A2I1GLK4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN ORFNames=RhiirA4_403467 {ECO:0000313|EMBL:PKY47495.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY47495.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY47495.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY47495.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005010}.
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:PKY47495.1}.
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DR EMBL; LLXI01000549; PKY47495.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FUN_019528; -.
DR VEuPathDB; FungiDB:GLOIN_2v1623991; -.
DR VEuPathDB; FungiDB:RhiirA1_424534; -.
DR OrthoDB; 5488444at2759; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000234323; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR028281; Sirohaem_synthase_central.
DR InterPro; IPR006367; Sirohaem_synthase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR01470; cysG_Nterm; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF13241; NAD_binding_7; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF14824; Sirohm_synth_M; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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:UP000234323}.
FT DOMAIN 917..1145
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1299 AA; 146614 MW; 7C897F893D5B9512 CRC64;
MTSTNGSLIV GWRLNGRHIL IIGGNQIASN RIEFALIAKP RKITLITPHN KITSDKIREH
IAKNNVSYKD SEFKPSDLIE SNNLPVDFVL SAVDNQQLSE QIANIAREKR IPVNIAEIPH
LCDFWFMPTY HDNHLQVAIS TNGTGPYVAR KLRQHIFENI PPNITAAINN VDLLKQNLGV
TNISAFTKII DTLPLSELTK LTSDDIKKLV SKHNVDDEEI EVSSTSESMD EKNSDVTIID
ERQDSGFTLK SKLFDVNGDV IIPSFTSGGT QLVDGKTAVE HIAYAFSTTS FIYPTTRTNY
VGKAALSWVS QKVPNAFGQS SQVIKMDTRY GASAAILGVM AHSRLDNVSI FATSQSIVPM
IPNFYGIVQA NIPLVIHVSA SGNDDQMINY VNYNDVLIAR ETGFGIINSY SSQEIHDIAL
ITHLISITTK TPFLHVFDGL NTSLELSKVN LLSYDSINNL IDEIKSLPIS STKNSDVLDC
FELIADKIGK LTGRQYRPFE YIGDPNAESI LVVLGGETVI TKETVKRINY GEKKVGIIIA
RVYRPWSEKH FLAVVPKTVK RIAILEQVAS KEDYSFGPSI FNDIAVSFSS DNSWINKSPI
LIDAKYLTTQ KFSPSVVHAI LKQLISNNNN IFNEELLLEK VNIPLINNNV KQCIFWDSET
QETIQAVKHI SKILEQHSKL NFTTSSTFDI YNNRGVITTN LQLGNDVISG LQDIESDYDF
ISVHDVSLTS KYNVLASAKN EAVVVLNTNW TVDELETKLP NDFRYEASKK NIKLFILNSE
KIAQDVGSTL KAVISVIFQS VFLRLFSNMI QLDCNLEDSI IDLFEGNNEK EASLLICAIC
QQLEKSIVSV ELPPTWGILE KSDQNLPSTI QSNSLDRNLD QPEIEKPKLR NWHVVAQNLL
FKEAYNFDRD IRPDLSEKTY IIRVSENRRL TPPSYDRYLF HIEFEIDGTD LKYDLGEALG
VYGHNDSKEV NQFLEFYGLN PDDVVFIPNK GNRFESRTIF QLFSQVLDIF GRPAKRFYES
LAQYATDEKE REKLLWMASN EGSQEFKRRV EDTITYAELL YEFTSAHPPI EDLVQLIAPI
KPRHYSIASA QSVHPNSVHL LVVTVEWENS KGVKRFGQCT RYLAGLKVGD SVTVSIKPSV
MKLPPRDTQP VIMAGLGTGM APFRAFIEER AYRKAQGKEV GPMVLYFGSR HRSMEYLYGE
ELEAYNIEGL LTHLRLAFSR DQENKVYIQH KMQEDSELLH QYLLKDEGWF YLCGPTWPVP
DVKDAIVNSF VTAGGYTSGQ AVDWVNKLKD LERYILEVY
//