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Database: UniProt
Entry: A0A062VU22_9MICO
LinkDB: A0A062VU22_9MICO
Original site: A0A062VU22_9MICO 
ID   A0A062VU22_9MICO        Unreviewed;       411 AA.
AC   A0A062VU22;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   13-SEP-2023, entry version 40.
DE   SubName: Full=Siroheme synthase CysG {ECO:0000313|EMBL:KDA05641.1};
GN   ORFNames=DC31_14470 {ECO:0000313|EMBL:KDA05641.1};
OS   Microbacterium sp. CH12i.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA05641.1, ECO:0000313|Proteomes:UP000027096};
RN   [1] {ECO:0000313|EMBL:KDA05641.1, ECO:0000313|Proteomes:UP000027096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH12i {ECO:0000313|EMBL:KDA05641.1,
RC   ECO:0000313|Proteomes:UP000027096};
RA   Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT   "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT   shallow groundwater in Cape Hallet, Antarctica.";
RL   Submitted (MAR-2014) 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|ARBA:ARBA00005879}.
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:KDA05641.1}.
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DR   EMBL; JHET01000007; KDA05641.1; -; Genomic_DNA.
DR   RefSeq; WP_036279317.1; NZ_JHET01000007.1.
DR   AlphaFoldDB; A0A062VU22; -.
DR   STRING; 1479651.DC31_14470; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00262; UER00222.
DR   Proteomes; UP000027096; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:InterPro.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR012409; Sirohaem_synth.
DR   InterPro; IPR006367; Sirohaem_synthase_N.
DR   NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR   NCBIfam; TIGR01470; cysG_Nterm; 1.
DR   PANTHER; PTHR45790:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF13241; NAD_binding_7; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036426; Sirohaem_synth; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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:UP000027096};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          167..373
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ   SEQUENCE   411 AA;  42884 MW;  3A3BB13331A64426 CRC64;
     MTTMIGLSLI GRQVLLVGGG VVAARRLGRF IADGAVVRLV APQLAPETRA LVIEHEIEWR
     ERRFRAPDID DVWIAHTATG DAAVDREVAA LCERNRVFCI NASDGAHSSA RMTAQTTSGD
     VVIGVVSEAG VDPRRTAGVR DAIESMLDAG QLPLRRRRIS HAGRVDLVGG GPGPIDLMTV
     RARRLLAEAD VVIADRLGPT AEVLAELDPD VLVVDVGKRP GHHLVAQEEI NALLVEHAAA
     GKRVVRLKGG DPFVYGRGGE EVIACQLAGI PVEVTPGPSS AISVPQAAGI PVTHRGTASS
     VLIVNGQGEV SATTLNGLGD SDVTTVMLMG VAALPKIVRA ARAHGISTDL PMAIIESGHT
     PRQRTTHCTL GTVLARAAEV GVANPAVIVF GDVARAGLLI PTPARVGDIR S
//
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