ID A0A165QJK0_9AGAM Unreviewed; 305 AA.
AC A0A165QJK0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN ORFNames=NEOLEDRAFT_1137980 {ECO:0000313|EMBL:KZT22509.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT22509.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT22509.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT22509.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR EMBL; KV425595; KZT22509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QJK0; -.
DR STRING; 1314782.A0A165QJK0; -.
DR InParanoid; A0A165QJK0; -.
DR OrthoDB; 296644at2759; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000076761; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004325; F:ferrochelatase activity; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR028161; Met8-like.
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 NCBIfam; TIGR01470; cysG_Nterm; 1.
DR PANTHER; PTHR35330; SIROHEME BIOSYNTHESIS PROTEIN MET8; 1.
DR PANTHER; PTHR35330:SF1; SIROHEME BIOSYNTHESIS PROTEIN MET8; 1.
DR Pfam; PF13241; NAD_binding_7; 1.
DR Pfam; PF14823; Sirohm_synth_C; 1.
DR Pfam; PF14824; Sirohm_synth_M; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 146..171
FT /note="Siroheme synthase central"
FT /evidence="ECO:0000259|Pfam:PF14824"
FT DOMAIN 174..244
FT /note="Siroheme biosynthesis protein Met8 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14823"
SQ SEQUENCE 305 AA; 32742 MW; 3688D65F5762C8C7 CRC64;
MAPDPTSLHG GSLLIAWQLT NKRVLIVGGG DVASGRLESV LVADANVTLV APAPLHPLTR
ELLDLLPERI TWHNREFQDS DLLLDPIDSH SNNPSPKYVA MVFTAIDSYR ESQRIAGLCH
DLRIPINAAD IPALCNFYFG SQVRSGALQI LVSTNGKSPK LANLIRKRIE SVIPPETADA
IENVGKLREK IKERAPGVGG PLSKRRMRWM VDLCGKWSME DLACLDNEMM AALVDGGWEK
GVVPGPNEVI GDKAPKANGH AQNGHAKATA DEIKGISLAE VAPVVGAFIV GALVSGLALL
GRARR
//
