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Database: UniProt
Entry: A0A177E1E7_ALTAL
LinkDB: A0A177E1E7_ALTAL
Original site: A0A177E1E7_ALTAL 
ID   A0A177E1E7_ALTAL        Unreviewed;       542 AA.
AC   A0A177E1E7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE            EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN   ORFNames=CC77DRAFT_6163 {ECO:0000313|EMBL:OAG25767.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG25767.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG25767.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG25767.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|RuleBase:RU003960}.
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DR   EMBL; KV441469; OAG25767.1; -; Genomic_DNA.
DR   RefSeq; XP_018391188.1; XM_018532457.1.
DR   AlphaFoldDB; A0A177E1E7; -.
DR   STRING; 5599.A0A177E1E7; -.
DR   GeneID; 29118051; -.
DR   KEGG; aalt:CC77DRAFT_6163; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_6163; -.
DR   OMA; TPCAIVE; -.
DR   OrthoDB; 296644at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:InterPro.
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; 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   PIRSF; PIRSF036555; SUMT_yeast; 2.
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   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:UP000077248};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          133..159
FT                   /note="Siroheme synthase central"
FT                   /evidence="ECO:0000259|Pfam:PF14824"
FT   DOMAIN          216..253
FT                   /note="Siroheme biosynthesis protein Met8 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14823"
FT   DOMAIN          273..480
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   542 AA;  58265 MW;  4750EFA65D493842 CRC64;
     MAPALLTAVD ATSHIHLVVG SNPLAGARCA RSIEVGAKPI LLAPEDSTLH YGLVKRIEVG
     EVKWLKRSFV EEDLTTLGRP EVDGVVDAVF VTAGGKHTSA THISSLCRRL RIPVNVADAP
     NLCSFTLLST HSDGPLQIGI TTSGKGCKLS ARIRREIAAS LPPRLGDAVE RLGTLRRRIW
     EEDHAAELSQ DLEAEEEDSG QPATFNKLIL EESKEAARGR RMRWLSQICE YWPLRRLAGI
     TDADVDMLFR EFASSSPSKV GPTATTPGRR AGRIILAGSG PGNPDLLTRA AHKAILSADL
     ILADKLVPAP ILDLVPRRAT VHIARKFPGN ADKAQEELLE LGLEGLKAGK VVVRIKQGDP
     YIYGRGGEEY DFFRAHGFIP SVLPGITSAL SAPLFAAIPA THRGIADQVL ICTGTGRKGA
     PLDPPEFVAS RTLVLLMSLH RLSALVESLV GKGYPAELPV AVLERASCPD QRVIRTTLEH
     VCAAVEEEGS RPPGLLVVGN ACKVLMKYEQ RWVVEEGFHG LDNLGGDGEL EISRLTEAAI
     AA
//
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